COVID-19: A Systematic Review of the Transmissibility, Pathogenesis, Entry Factors, and Signature Immune Response
Abstract
:1. Introduction
2. Materials and Methods
2.1. Eligibility Criteria
2.2. Information Sources
2.3. Study Selection
2.4. Data Extraction
2.5. Assessment of Risk of Bias
3. Results
3.1. Viral Transmissibility
3.2. Pathophysiology
3.3. SARS-CoV-2 Entry Factors
3.4. ACE2 Receptor
3.5. Immune Response
3.6. SARS-CoV-2 Variants
4. Discussion
5. Conclusions
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
- Ganesh, B.; Rajakumar, T.; Malathi, M.; Manikandan, N.; Nagaraj, J.; Santhakumar, A.; Elangovan, A.; Malik, Y.S. Epidemiology and pathobiology of SARS-CoV-2 (COVID-19) in comparison with SARS, MERS: An updated overview of current knowledge and future perspectives. Clin. Epidemiol. Glob. Health 2021, 10, 100694. [Google Scholar] [CrossRef] [PubMed]
- World Health Organization. WHO Coronavirus (COVID-19) Dashboard. Available online: https://covid19.who.int/ (accessed on 7 March 2022).
- Nicola, M.; Alsafi, Z.; Sohrabi, C.; Kerwan, A.; Al-Jabir, A.; Iosifidis, C.; Agha, M.; Agha, R. The socio-economic implications of the coronavirus pandemic (COVID-19): A review. Int. J. Surg. 2020, 78, 185–193. [Google Scholar] [CrossRef] [PubMed]
- Cascella, M.; Rajnik, M.; Aleem, A.; Dulebohn, S.C.; Di Napoli, R. Features, Evaluation, and Treatment of Coronavirus (COVID-19). In StatPearls; StatPearls Publishing: Treasure Island, FL, USA, 2021. [Google Scholar]
- Jain, V.K.; Iyengar, K.P.; Vaishya, R. Differences between First wave and Second wave of COVID-19 in India. Diabetes Metab. Syndr. Clin. Res. Rev. 2021, 15, 1047–1048. [Google Scholar] [CrossRef] [PubMed]
- Chan, J.F.; Yuan, S.; Kok, K.H.; To, K.K.; Chu, H.; Yang, J.; Xing, F.; Liu, J.; Yip, C.C.; Poon, R.W.; et al. A familial cluster of pneumonia associated with the 2019 novel coronavirus indicating person-to-person transmission: A study of a family cluster. Lancet 2020, 395, 514–523. [Google Scholar] [CrossRef] [Green Version]
- Karia, R.; Gupta, I.; Khandait, H.; Yadav, A.; Yadav, A. COVID-19 and its Modes of Transmission. SN Compr. Clin. Med. 2020, 2, 1798–1801. [Google Scholar] [CrossRef] [PubMed]
- Harrison, A.G.; Lin, T.; Wang, P. Mechanisms of SARS-CoV-2 Transmission and Pathogenesis. Trends Immunol. 2020, 41, 1100–1115. [Google Scholar] [CrossRef]
- Lewis, D. Is the coronavirus airborne? Experts can’t agree. Nature 2020, 580, 175. [Google Scholar] [CrossRef] [Green Version]
- Lui, G.; Ling, L.; Lai, C.K.; Tso, E.Y.; Fung, K.S.; Chan, V.; Ho, T.H.; Luk, F.; Chen, Z.; Ng, J.K.; et al. Viral dynamics of SARS-CoV-2 across a spectrum of disease severity in COVID-19. J. Infect. 2020, 81, 318–356. [Google Scholar] [CrossRef]
- Santarpia, J.L.; Rivera, D.N.; Herrera, V.L.; Morwitzer, M.J.; Creager, H.M.; Santarpia, G.W.; Crown, K.K.; Brett-Major, D.M.; Schnaubelt, E.R.; Broadhurst, M.J.; et al. Aerosol and surface contamination of SARS-CoV-2 observed in quarantine and isolation care. Sci. Rep. 2020, 10, 12732. [Google Scholar] [CrossRef]
- Goldman, E. Exaggerated risk of transmission of COVID-19 by fomites. Lancet Infect. Dis. 2020, 20, 892–893. [Google Scholar] [CrossRef]
- Mondelli, M.U.; Colaneri, M.; Seminari, E.M.; Baldanti, F.; Bruno, R. Low risk of SARS-CoV-2 transmission by fomites in real-life conditions. Lancet Infect. Dis. 2021, 21, e112. [Google Scholar] [CrossRef]
- van Doremalen, N.; Bushmaker, T.; Morris, D.H.; Holbrook, M.G.; Gamble, A.; Williamson, B.N.; Tamin, A.; Harcourt, J.L.; Thornburg, N.J.; Gerber, S.I.; et al. Aerosol and Surface Stability of SARS-CoV-2 as Compared with SARS-CoV-1. N. Engl. J. Med. 2020, 382, 1564–1567. [Google Scholar] [CrossRef] [PubMed]
- Chen, Y.; Chen, L.; Deng, Q.; Zhang, G.; Wu, K.; Ni, L.; Yang, Y.; Liu, B.; Wang, W.; Wei, C.; et al. The presence of SARS-CoV-2 RNA in the feces of COVID-19 patients. J. Med. Virol. 2020, 92, 833–840. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hindson, J. COVID-19: Faecal-oral transmission? Nat. Rev. Gastroenterol. Hepatol. 2020, 17, 259. [Google Scholar] [CrossRef]
- Wu, Y.; Guo, C.; Tang, L.; Hong, Z.; Zhou, J.; Dong, X.; Yin, H.; Xiao, Q.; Tang, Y.; Qu, X.; et al. Prolonged presence of SARS-CoV-2 viral RNA in faecal samples. Lancet Gastroenterol. Hepatol. 2020, 5, 434–435. [Google Scholar] [CrossRef]
- Zheng, X.; Chen, J.; Deng, L.; Fang, Z.; Chen, G.; Ye, D.; Xia, J.; Hong, Z. Risk factors for the COVID-19 severity and its correlation with viral shedding: A retrospective cohort study. J. Med. Virol. 2021, 93, 952–961. [Google Scholar] [CrossRef]
- Xu, Y.; Li, X.; Zhu, B.; Liang, H.; Fang, C.; Gong, Y.; Guo, Q.; Sun, X.; Zhao, D.; Shen, J.; et al. Characteristics of pediatric SARS-CoV-2 infection and potential evidence for persistent fecal viral shedding. Nat. Med. 2020, 26, 502–505. [Google Scholar] [CrossRef] [Green Version]
- Kawasuji, H.; Takegoshi, Y.; Kaneda, M.; Ueno, A.; Miyajima, Y.; Kawago, K.; Fukui, Y.; Yoshida, Y.; Kimura, M.; Yamada, H.; et al. Transmissibility of COVID-19 depends on the viral load around onset in adult and symptomatic patients. PLoS ONE 2020, 15, e0243597. [Google Scholar] [CrossRef]
- Nishiura, H.; Linton, N.M.; Akhmetzhanov, A.R. Serial interval of novel coronavirus (COVID-19) infections. Int. J. Infect. Dis. 2020, 93, 284–286. [Google Scholar] [CrossRef]
- Zhang, M.; Xiao, J.; Deng, A.; Zhang, Y.; Zhuang, Y.; Hu, T.; Li, J.; Tu, H.; Li, B.; Zhou, Y.; et al. Transmission Dynamics of an Outbreak of the COVID-19 Delta Variant B.1.617.2—Guangdong Province, China, May-June 2021. China CDC Wkly. 2021, 3, 584–586. [Google Scholar] [CrossRef]
- Ryu, S.; Kim, D.; Lim, J.S.; Ali, S.T.; Cowling, B.J. Serial Interval and Transmission Dynamics during SARS-CoV-2 Delta Variant Predominance, South Korea. Emerg. Infect. Dis. 2022, 28, 407–410. [Google Scholar] [CrossRef] [PubMed]
- He, X.; Lau, E.H.Y.; Wu, P.; Deng, X.; Wang, J.; Hao, X.; Lau, Y.C.; Wong, J.Y.; Guan, Y.; Tan, X.; et al. Author Correction: Temporal dynamics in viral shedding and transmissibility of COVID-19. Nat. Med. 2020, 26, 1491–1493. [Google Scholar] [CrossRef] [PubMed]
- To, K.K.; Tsang, O.T.; Leung, W.S.; Tam, A.R.; Wu, T.C.; Lung, D.C.; Yip, C.C.; Cai, J.P.; Chan, J.M.; Chik, T.S.; et al. Temporal profiles of viral load in posterior oropharyngeal saliva samples and serum antibody responses during infection by SARS-CoV-2: An observational cohort study. Lancet Infect. Dis. 2020, 20, 565–574. [Google Scholar] [CrossRef] [Green Version]
- Zou, L.; Ruan, F.; Huang, M.; Liang, L.; Huang, H.; Hong, Z.; Yu, J.; Kang, M.; Song, Y.; Xia, J.; et al. SARS-CoV-2 Viral Load in Upper Respiratory Specimens of Infected Patients. N. Engl. J. Med. 2020, 382, 1177–1179. [Google Scholar] [CrossRef] [PubMed]
- Liu, Y.; Ning, Z.; Chen, Y.; Guo, M.; Liu, Y.; Gali, N.K.; Sun, L.; Duan, Y.; Cai, J.; Westerdahl, D.; et al. Aerodynamic analysis of SARS-CoV-2 in two Wuhan hospitals. Nature 2020, 582, 557–560. [Google Scholar] [CrossRef]
- Zhao, L.P.; Roychoudhury, P.; Gilbert, P.; Schiffer, J.; Lybrand, T.P.; Payne, T.H.; Randhawa, A.; Thiebaud, S.; Mills, M.; Greninger, A.; et al. Mutations in viral nucleocapsid protein and endoRNase are discovered to associate with COVID19 hospitalization risk. Sci. Rep. 2022, 12, 1206. [Google Scholar] [CrossRef] [PubMed]
- Zeng, W.; Liu, G.; Ma, H.; Zhao, D.; Yang, Y.; Liu, M.; Mohammed, A.; Zhao, C.; Yang, Y.; Xie, J.; et al. Biochemical characterization of SARS-CoV-2 nucleocapsid protein. Biochem. Biophys. Res. Commun. 2020, 527, 618–623. [Google Scholar] [CrossRef] [PubMed]
- Hasanoglu, I.; Korukluoglu, G.; Asilturk, D.; Cosgun, Y.; Kalem, A.K.; Altas, A.B.; Kayaaslan, B.; Eser, F.; Kuzucu, E.A.; Guner, R. Higher viral loads in asymptomatic COVID-19 patients might be the invisible part of the iceberg. Infection 2021, 49, 117–126. [Google Scholar] [CrossRef] [PubMed]
- Li, T.Z.; Cao, Z.H.; Chen, Y.; Cai, M.T.; Zhang, L.Y.; Xu, H.; Zhang, J.Y.; Ma, C.H.; Liu, Y.; Gao, L.J.; et al. Duration of SARS-CoV-2 RNA shedding and factors associated with prolonged viral shedding in patients with COVID-19. J. Med. Virol. 2021, 93, 506–512. [Google Scholar] [CrossRef]
- Tan, W.; Lu, Y.; Zhang, J.; Wang, J.; Dan, Y.; Tan, Z.; He, X.; Qian, C.; Sun, Q.; Hu, Q.; et al. Viral Kinetics and Antibody Responses in Patients with COVID-19. medRxiv 2020. [Google Scholar] [CrossRef] [Green Version]
- Xu, K.; Chen, Y.; Yuan, J.; Yi, P.; Ding, C.; Wu, W.; Li, Y.; Ni, Q.; Zou, R.; Li, X.; et al. Factors Associated With Prolonged Viral RNA Shedding in Patients with Coronavirus Disease 2019 (COVID-19). Clin. Infect. Dis. 2020, 71, 799–806. [Google Scholar] [CrossRef] [PubMed]
- Fang, Z.; Zhang, Y.; Hang, C.; Ai, J.; Li, S.; Zhang, W. Comparisons of viral shedding time of SARS-CoV-2 of different samples in ICU and non-ICU patients. J. Infect. 2020, 81, 147–178. [Google Scholar] [CrossRef] [PubMed]
- Fajnzylber, J.; Regan, J.; Coxen, K.; Corry, H.; Wong, C.; Rosenthal, A.; Worrall, D.; Giguel, F.; Piechocka-Trocha, A.; Atyeo, C.; et al. SARS-CoV-2 viral load is associated with increased disease severity and mortality. Nat. Commun. 2020, 11, 5493. [Google Scholar] [CrossRef] [PubMed]
- Pujadas, E.; Chaudhry, F.; McBride, R.; Richter, F.; Zhao, S.; Wajnberg, A.; Nadkarni, G.; Glicksberg, B.S.; Houldsworth, J.; Cordon-Cardo, C. SARS-CoV-2 viral load predicts COVID-19 mortality. Lancet Respir. Med. 2020, 8, e70. [Google Scholar] [CrossRef]
- Zhou, B.; She, J.; Wang, Y.; Ma, X. Duration of Viral Shedding of Discharged Patients with Severe COVID-19. Clin. Infect. Dis. 2020, 71, 2240–2242. [Google Scholar] [CrossRef]
- Wang, K.; Zhang, X.; Sun, J.; Ye, J.; Wang, F.; Hua, J.; Zhang, H.; Shi, T.; Li, Q.; Wu, X. Differences of Severe Acute Respiratory Syndrome Coronavirus 2 Shedding Duration in Sputum and Nasopharyngeal Swab Specimens Among Adult Inpatients With Coronavirus Disease 2019. Chest 2020, 158, 1876–1884. [Google Scholar] [CrossRef]
- Lan, L.; Xu, D.; Ye, G.; Xia, C.; Wang, S.; Li, Y.; Xu, H. Positive RT-PCR Test Results in Patients Recovered from COVID-19. JAMA 2020, 323, 1502–1503. [Google Scholar] [CrossRef] [Green Version]
- Lang, R.; Benham, J.L.; Atabati, O.; Hollis, A.; Tombe, T.; Shaffer, B.; Burns, K.K.; MacKean, G.; Leveille, T.; McCormack, B.; et al. Attitudes, behaviours and barriers to public health measures for COVID-19: A survey to inform public health messaging. BMC Public Health 2021, 21, 765. [Google Scholar] [CrossRef]
- Ge, Y.; Martinez, L.; Sun, S.; Chen, Z.; Zhang, F.; Li, F.; Sun, W.; Chen, E.; Pan, J.; Li, C.; et al. COVID-19 Transmission Dynamics Among Close Contacts of Index Patients With COVID-19: A Population-Based Cohort Study in Zhejiang Province, China. JAMA Intern. Med. 2021, 181, 1343–1350. [Google Scholar] [CrossRef]
- Liang, J.; Yuan, H.-Y. Assessing the impact of temperature and humidity exposures during early infection stages on case-fatality of COVID-19: A modelling study in Europe. Environ. Res. 2022, 211, 112931. [Google Scholar] [CrossRef]
- Ogata, T.; Tanaka, H. Long Diagnostic Delay with Unknown Transmission Route Inversely Correlates with the Subsequent Doubling Time of Coronavirus Disease 2019 in Japan, February–March 2020. Int. J. Environ. Res. Public Health 2021, 18, 3377. [Google Scholar] [CrossRef] [PubMed]
- Han, J.; Shi, L.X.; Xie, Y.; Zhang, Y.J.; Huang, S.P.; Li, J.G.; Wang, H.R.; Shao, S.F. Analysis of factors affecting the prognosis of COVID-19 patients and viral shedding duration. Epidemiol. Infect. 2020, 148, e125. [Google Scholar] [CrossRef] [PubMed]
- Li, S.; Hu, Z.; Song, X. High-dose but Not Low-dose Corticosteroids Potentially Delay Viral Shedding of Patients with COVID-19. Clin. Infect. Dis. 2021, 72, 1297–1298. [Google Scholar] [CrossRef] [PubMed]
- Hosoki, K.; Chakraborty, A.; Sur, S. Molecular mechanisms and epidemiology of COVID-19 from an allergist’s perspective. J. Allergy Clin. Immunol. 2020, 146, 285–299. [Google Scholar] [CrossRef] [PubMed]
- Masters, P.S. The molecular biology of coronaviruses. Adv. Virus Res. 2006, 66, 193–292. [Google Scholar] [CrossRef] [PubMed]
- Pillay, T.S. Gene of the month: The 2019-nCoV/SARS-CoV-2 novel coronavirus spike protein. J. Clin. Pathol. 2020, 73, 366–369. [Google Scholar] [CrossRef] [PubMed]
- Hoffmann, M.; Kleine-Weber, H.; Pohlmann, S. A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells. Mol. Cell 2020, 78, 779–784.e5. [Google Scholar] [CrossRef]
- Walls, A.C.; Park, Y.J.; Tortorici, M.A.; Wall, A.; McGuire, A.T.; Veesler, D. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell 2020, 183, 1735. [Google Scholar] [CrossRef]
- Wrapp, D.; Wang, N.; Corbett, K.S.; Goldsmith, J.A.; Hsieh, C.L.; Abiona, O.; Graham, B.S.; McLellan, J.S. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science 2020, 367, 1260–1263. [Google Scholar] [CrossRef] [Green Version]
- Wang, Q.; Zhang, Y.; Wu, L.; Niu, S.; Song, C.; Zhang, Z.; Lu, G.; Qiao, C.; Hu, Y.; Yuen, K.Y.; et al. Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2. Cell 2020, 181, 894–904.e9. [Google Scholar] [CrossRef]
- Li, F.; Li, W.; Farzan, M.; Harrison, S.C. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 2005, 309, 1864–1868. [Google Scholar] [CrossRef] [PubMed]
- Li, W.; Zhang, C.; Sui, J.; Kuhn, J.H.; Moore, M.J.; Luo, S.; Wong, S.K.; Huang, I.C.; Xu, K.; Vasilieva, N.; et al. Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2. EMBO J. 2005, 24, 1634–1643. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Shang, J.; Ye, G.; Shi, K.; Wan, Y.; Luo, C.; Aihara, H.; Geng, Q.; Auerbach, A.; Li, F. Structural basis of receptor recognition by SARS-CoV-2. Nature 2020, 581, 221–224. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hoffmann, M.; Hofmann-Winkler, H.; Pöhlmann, S. Priming Time: How Cellular Proteases Arm Coronavirus Spike Proteins. In Activation of Viruses by Host Proteases; Springer: Cham, Switzerland, 2018; pp. 71–98. [Google Scholar]
- Belouzard, S.; Chu, V.C.; Whittaker, G.R. Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. Proc. Natl. Acad. Sci. USA 2009, 106, 5871–5876. [Google Scholar] [CrossRef] [Green Version]
- Millet, J.K.; Whittaker, G.R. Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein. Proc. Natl. Acad. Sci. USA 2014, 111, 15214–15219. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Coronaviridae Study Group of the International Committee on Taxonomy of Viruses. The species Severe acute respiratory syndrome-related coronavirus: Classifying 2019-nCoV and naming it SARS-CoV-2. Nat. Microbiol. 2020, 5, 536–544. [Google Scholar] [CrossRef] [Green Version]
- Lu, R.; Zhao, X.; Li, J.; Niu, P.; Yang, B.; Wu, H.; Wang, W.; Song, H.; Huang, B.; Zhu, N.; et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: Implications for virus origins and receptor binding. Lancet 2020, 395, 565–574. [Google Scholar] [CrossRef] [Green Version]
- Wacharapluesadee, S.; Tan, C.W.; Maneeorn, P.; Duengkae, P.; Zhu, F.; Joyjinda, Y.; Kaewpom, T.; Chia, W.N.; Ampoot, W.; Lim, B.L.; et al. Evidence for SARS-CoV-2 related coronaviruses circulating in bats and pangolins in Southeast Asia. Nat. Commun. 2021, 12, 972. [Google Scholar] [CrossRef]
- Zhou, P.; Yang, X.L.; Wang, X.G.; Hu, B.; Zhang, L.; Zhang, W.; Si, H.R.; Zhu, Y.; Li, B.; Huang, C.L.; et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 2020, 579, 270–273. [Google Scholar] [CrossRef] [Green Version]
- da Rosa Mesquita, R.; Francelino Silva Junior, L.C.; Santos Santana, F.M.; Farias de Oliveira, T.; Campos Alcantara, R.; Monteiro Arnozo, G.; Rodrigues da Silva Filho, E.; Galdino Dos Santos, A.G.; Oliveira da Cunha, E.J.; Salgueiro de Aquino, S.H.; et al. Clinical manifestations of COVID-19 in the general population: Systematic review. Wien. Klin. Wochenschr. 2021, 133, 377–382. [Google Scholar] [CrossRef]
- Huang, C.; Wang, Y.; Li, X.; Ren, L.; Zhao, J.; Hu, Y.; Zhang, L.; Fan, G.; Xu, J.; Gu, X.; et al. Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China. Lancet 2020, 395, 497–506. [Google Scholar] [CrossRef] [Green Version]
- Stokes, E.K.; Zambrano, L.D.; Anderson, K.N.; Marder, E.P.; Raz, K.M.; El Burai Felix, S.; Tie, Y.; Fullerton, K.E. Coronavirus Disease 2019 Case Surveillance—United States, January 22–May 30, 2020. MMWR Morb. Mortal. Wkly. Rep. 2020, 69, 759–765. [Google Scholar] [CrossRef] [PubMed]
- Guan, W.J.; Ni, Z.Y.; Hu, Y.; Liang, W.H.; Ou, C.Q.; He, J.X.; Liu, L.; Shan, H.; Lei, C.L.; Hui, D.S.C.; et al. Clinical Characteristics of Coronavirus Disease 2019 in China. N. Engl. J. Med. 2020, 382, 1708–1720. [Google Scholar] [CrossRef] [PubMed]
- Wang, D.; Hu, B.; Hu, C.; Zhu, F.; Liu, X.; Zhang, J.; Wang, B.; Xiang, H.; Cheng, Z.; Xiong, Y.; et al. Clinical Characteristics of 138 Hospitalized Patients With 2019 Novel Coronavirus-Infected Pneumonia in Wuhan, China. JAMA 2020, 323, 1061–1069. [Google Scholar] [CrossRef] [PubMed]
- Zhang, J.J.; Dong, X.; Cao, Y.Y.; Yuan, Y.D.; Yang, Y.B.; Yan, Y.Q.; Akdis, C.A.; Gao, Y.D. Clinical characteristics of 140 patients infected with SARS-CoV-2 in Wuhan, China. Allergy 2020, 75, 1730–1741. [Google Scholar] [CrossRef] [PubMed]
- Caronna, E.; Ballve, A.; Llaurado, A.; Gallardo, V.J.; Ariton, D.M.; Lallana, S.; Lopez Maza, S.; Olive Gadea, M.; Quibus, L.; Restrepo, J.L.; et al. Headache: A striking prodromal and persistent symptom, predictive of COVID-19 clinical evolution. Cephalalgia 2020, 40, 1410–1421. [Google Scholar] [CrossRef]
- Uygun, O.; Ertas, M.; Ekizoglu, E.; Bolay, H.; Ozge, A.; Kocasoy Orhan, E.; Cagatay, A.A.; Baykan, B. Headache characteristics in COVID-19 pandemic-a survey study. J. Headache Pain 2020, 21, 121. [Google Scholar] [CrossRef]
- Porta-Etessam, J.; Matias-Guiu, J.A.; Gonzalez-Garcia, N.; Gomez Iglesias, P.; Santos-Bueso, E.; Arriola-Villalobos, P.; Garcia-Azorin, D.; Matias-Guiu, J. Spectrum of Headaches Associated With SARS-CoV-2 Infection: Study of Healthcare Professionals. Headache 2020, 60, 1697–1704. [Google Scholar] [CrossRef]
- Bolay, H.; Gul, A.; Baykan, B. COVID-19 is a Real Headache! Headache 2020, 60, 1415–1421. [Google Scholar] [CrossRef]
- Bobker, S.M.; Robbins, M.S. COVID-19 and Headache: A Primer for Trainees. Headache 2020, 60, 1806–1811. [Google Scholar] [CrossRef]
- Chung, T.W.; Sridhar, S.; Zhang, A.J.; Chan, K.H.; Li, H.L.; Wong, F.K.; Ng, M.Y.; Tsang, R.K.; Lee, A.C.; Fan, Z.; et al. Olfactory Dysfunction in Coronavirus Disease 2019 Patients: Observational Cohort Study and Systematic Review. Open Forum Infect. Dis. 2020, 7, ofaa199. [Google Scholar] [CrossRef] [PubMed]
- Tong, J.Y.; Wong, A.; Zhu, D.; Fastenberg, J.H.; Tham, T. The Prevalence of Olfactory and Gustatory Dysfunction in COVID-19 Patients: A Systematic Review and Meta-analysis. Otolaryngol. Head Neck Surg. 2020, 163, 3–11. [Google Scholar] [CrossRef] [PubMed]
- Marzano, A.V.; Genovese, G.; Fabbrocini, G.; Pigatto, P.; Monfrecola, G.; Piraccini, B.M.; Veraldi, S.; Rubegni, P.; Cusini, M.; Caputo, V.; et al. Varicella-like exanthem as a specific COVID-19-associated skin manifestation: Multicenter case series of 22 patients. J. Am. Acad. Dermatol. 2020, 83, 280–285. [Google Scholar] [CrossRef] [PubMed]
- Recalcati, S. Cutaneous manifestations in COVID-19: A first perspective. J. Eur. Acad. Dermatol. Venereol. 2020, 34, e212–e213. [Google Scholar] [CrossRef] [PubMed]
- Kordzadeh-Kermani, E.; Khalili, H.; Karimzadeh, I. Pathogenesis, clinical manifestations and complications of coronavirus disease 2019 (COVID-19). Future Microbiol. 2020, 15, 1287–1305. [Google Scholar] [CrossRef]
- Tsai, P.H.; Lai, W.Y.; Lin, Y.Y.; Luo, Y.H.; Lin, Y.T.; Chen, H.K.; Chen, Y.M.; Lai, Y.C.; Kuo, L.C.; Chen, S.D.; et al. Clinical manifestation and disease progression in COVID-19 infection. J. Chin. Med. Assoc. 2021, 84, 3–8. [Google Scholar] [CrossRef]
- Zupin, L.; Fontana, F.; Gratton, R.; Milani, M.; Clemente, L.; Pascolo, L.; Ruscio, M.; Crovella, S. SARS-CoV-2 Short-Time Infection Produces Relevant Cytopathic Effects in Vero E6 Cell Line. Int. J. Environ. Res. Public Health 2021, 18, 9020. [Google Scholar] [CrossRef]
- Velavan, T.P.; Meyer, C.G. Mild versus severe COVID-19: Laboratory markers. Int. J. Infect. Dis. 2020, 95, 304–307. [Google Scholar] [CrossRef]
- van Eijk, L.E.; Binkhorst, M.; Bourgonje, A.R.; Offringa, A.K.; Mulder, D.J.; Bos, E.M.; Kolundzic, N.; Abdulle, A.E.; van der Voort, P.H.; Olde Rikkert, M.G.; et al. COVID-19: Immunopathology, pathophysiological mechanisms, and treatment options. J. Pathol. 2021, 254, 307–331. [Google Scholar] [CrossRef]
- Williamson, E.J.; Walker, A.J.; Bhaskaran, K.; Bacon, S.; Bates, C.; Morton, C.E.; Curtis, H.J.; Mehrkar, A.; Evans, D.; Inglesby, P.; et al. Factors associated with COVID-19-related death using OpenSAFELY. Nature 2020, 584, 430–436. [Google Scholar] [CrossRef]
- Binkhorst, M.; Offringa, A.K.; van der Hoeven, J.G. COVID-19: Comprehensive Synopsis of Suggested Pathophysiological Mechanisms and Repurposed Drugs. Preprints 2020, 2020070108. [Google Scholar] [CrossRef]
- Bao, J.; Li, C.; Zhang, K.; Kang, H.; Chen, W.; Gu, B. Comparative analysis of laboratory indexes of severe and non-severe patients infected with COVID-19. Clin. Chim. Acta 2020, 509, 180–194. [Google Scholar] [CrossRef] [PubMed]
- Wright, F.L.; Vogler, T.O.; Moore, E.E.; Moore, H.B.; Wohlauer, M.V.; Urban, S.; Nydam, T.L.; Moore, P.K.; McIntyre, R.C., Jr. Fibrinolysis Shutdown Correlation with Thromboembolic Events in Severe COVID-19 Infection. J. Am. Coll. Surg. 2020, 231, 193–203.e1. [Google Scholar] [CrossRef] [PubMed]
- Tang, N.; Li, D.; Wang, X.; Sun, Z. Abnormal coagulation parameters are associated with poor prognosis in patients with novel coronavirus pneumonia. J. Thromb. Haemost. 2020, 18, 844–847. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Huertas, A.; Montani, D.; Savale, L.; Pichon, J.; Tu, L.; Parent, F.; Guignabert, C.; Humbert, M. Endothelial cell dysfunction: A major player in SARS-CoV-2 infection (COVID-19)? Eur. Respir. J. 2020, 56, 2001634. [Google Scholar] [CrossRef] [PubMed]
- Tay, M.Z.; Poh, C.M.; Renia, L.; MacAry, P.A.; Ng, L.F.P. The trinity of COVID-19: Immunity, inflammation and intervention. Nat. Rev. Immunol. 2020, 20, 363–374. [Google Scholar] [CrossRef]
- Loo, J.; Spittle, D.A.; Newnham, M. COVID-19, immunothrombosis and venous thromboembolism: Biological mechanisms. Thorax 2021, 76, 412–420. [Google Scholar] [CrossRef]
- Hoffmann, M.; Kleine-Weber, H.; Schroeder, S.; Kruger, N.; Herrler, T.; Erichsen, S.; Schiergens, T.S.; Herrler, G.; Wu, N.H.; Nitsche, A.; et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell 2020, 181, 271–280.e8. [Google Scholar] [CrossRef]
- Valyaeva, A.A.; Zharikova, A.A.; Kasianov, A.S.; Vassetzky, Y.S.; Sheval, E.V. Expression of SARS-CoV-2 entry factors in lung epithelial stem cells and its potential implications for COVID-19. Sci. Rep. 2020, 10, 17772. [Google Scholar] [CrossRef]
- Cevik, M.; Kuppalli, K.; Kindrachuk, J.; Peiris, M. Virology, transmission, and pathogenesis of SARS-CoV-2. BMJ 2020, 371, m3862. [Google Scholar] [CrossRef]
- Domingo, P.; Mur, I.; Pomar, V.; Corominas, H.; Casademont, J.; de Benito, N. The four horsemen of a viral Apocalypse: The pathogenesis of SARS-CoV-2 infection (COVID-19). EBioMedicine 2020, 58, 102887. [Google Scholar] [CrossRef] [PubMed]
- Imai, Y.; Kuba, K.; Penninger, J.M. The discovery of angiotensin-converting enzyme 2 and its role in acute lung injury in mice. Exp. Physiol. 2008, 93, 543–548. [Google Scholar] [CrossRef] [PubMed]
- Perlot, T.; Penninger, J.M. ACE2—From the renin-angiotensin system to gut microbiota and malnutrition. Microbes Infect. 2013, 15, 866–873. [Google Scholar] [CrossRef] [PubMed]
- Silhol, F.; Sarlon, G.; Deharo, J.C.; Vaisse, B. Downregulation of ACE2 induces overstimulation of the renin-angiotensin system in COVID-19: Should we block the renin-angiotensin system? Hypertens. Res. 2020, 43, 854–856. [Google Scholar] [CrossRef] [PubMed]
- Bader, M. ACE2, angiotensin-(1–7), and Mas: The other side of the coin. Pflugers Arch. 2013, 465, 79–85. [Google Scholar] [CrossRef] [PubMed]
- Gaddam, R.R.; Chambers, S.; Bhatia, M. ACE and ACE2 in inflammation: A tale of two enzymes. Inflamm. Allergy Drug Targets 2014, 13, 224–234. [Google Scholar] [CrossRef]
- Moore, J.B.; June, C.H. Cytokine release syndrome in severe COVID-19. Science 2020, 368, 473–474. [Google Scholar] [CrossRef] [Green Version]
- Reis, R.F.; Pigozzo, A.B.; Bonin, C.R.B.; Quintela, B.M.; Pompei, L.T.; Vieira, A.C.; Silva, L.L.E.; Xavier, M.P.; Weber Dos Santos, R.; Lobosco, M. A Validated Mathematical Model of the Cytokine Release Syndrome in Severe COVID-19. Front. Mol. Biosci. 2021, 8, 639423. [Google Scholar] [CrossRef]
- Sanchez-Martinez, F.; Arenas-Miras, M.; Jove-Caballe, N.; Knobel-Freud, H.; on behalf of COVID-19 Infectious Disease Team Hospital del Mar. Influence of Cytokine Release Syndrome in Severe COVID-19 Patients Treated With Tocilizumab Over the Quantiferon TB Gold Plus Results. Arch. Bronconeumol. 2021, 57 (Suppl. 2), 58–59. [Google Scholar] [CrossRef]
- Drosten, C.; Seilmaier, M.; Corman, V.M.; Hartmann, W.; Scheible, G.; Sack, S.; Guggemos, W.; Kallies, R.; Muth, D.; Junglen, S.; et al. Clinical features and virological analysis of a case of Middle East respiratory syndrome coronavirus infection. Lancet Infect. Dis. 2013, 13, 745–751. [Google Scholar] [CrossRef] [Green Version]
- Zhang, B.; Zhou, X.; Qiu, Y.; Song, Y.; Feng, F.; Feng, J.; Song, Q.; Jia, Q.; Wang, J. Clinical characteristics of 82 cases of death from COVID-19. PLoS ONE 2020, 15, e0235458. [Google Scholar] [CrossRef] [PubMed]
- Hojyo, S.; Uchida, M.; Tanaka, K.; Hasebe, R.; Tanaka, Y.; Murakami, M.; Hirano, T. How COVID-19 induces cytokine storm with high mortality. Inflamm. Regen. 2020, 40, 37. [Google Scholar] [CrossRef] [PubMed]
- Channappanavar, R.; Fehr, A.R.; Vijay, R.; Mack, M.; Zhao, J.; Meyerholz, D.K.; Perlman, S. Dysregulated Type I Interferon and Inflammatory Monocyte-Macrophage Responses Cause Lethal Pneumonia in SARS-CoV-Infected Mice. Cell Host Microbe 2016, 19, 181–193. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Law, H.K.; Cheung, C.Y.; Ng, H.Y.; Sia, S.F.; Chan, Y.O.; Luk, W.; Nicholls, J.M.; Peiris, J.S.; Lau, Y.L. Chemokine up-regulation in SARS-coronavirus-infected, monocyte-derived human dendritic cells. Blood 2005, 106, 2366–2374. [Google Scholar] [CrossRef] [Green Version]
- Spiegel, M.; Schneider, K.; Weber, F.; Weidmann, M.; Hufert, F.T. Interaction of severe acute respiratory syndrome-associated coronavirus with dendritic cells. J. Gen. Virol. 2006, 87, 1953–1960. [Google Scholar] [CrossRef]
- Yen, Y.T.; Liao, F.; Hsiao, C.H.; Kao, C.L.; Chen, Y.C.; Wu-Hsieh, B.A. Modeling the early events of severe acute respiratory syndrome coronavirus infection in vitro. J. Virol. 2006, 80, 2684–2693. [Google Scholar] [CrossRef] [Green Version]
- Blanco-Melo, D.; Nilsson-Payant, B.E.; Liu, W.C.; Uhl, S.; Hoagland, D.; Moller, R.; Jordan, T.X.; Oishi, K.; Panis, M.; Sachs, D.; et al. Imbalanced Host Response to SARS-CoV-2 Drives Development of COVID-19. Cell 2020, 181, 1036–1045.e9. [Google Scholar] [CrossRef]
- Hadjadj, J.; Yatim, N.; Barnabei, L.; Corneau, A.; Boussier, J.; Smith, N.; Pere, H.; Charbit, B.; Bondet, V.; Chenevier-Gobeaux, C.; et al. Impaired type I interferon activity and inflammatory responses in severe COVID-19 patients. Science 2020, 369, 718–724. [Google Scholar] [CrossRef]
- Zhang, Q.; Bastard, P.; Liu, Z.; Le Pen, J.; Moncada-Velez, M.; Chen, J.; Ogishi, M.; Sabli, I.K.D.; Hodeib, S.; Korol, C.; et al. Inborn errors of type I IFN immunity in patients with life-threatening COVID-19. Science 2020, 370, eabd4570. [Google Scholar] [CrossRef]
- Bastard, P.; Rosen, L.B.; Zhang, Q.; Michailidis, E.; Hoffmann, H.H.; Zhang, Y.; Dorgham, K.; Philippot, Q.; Rosain, J.; Beziat, V.; et al. Autoantibodies against type I IFNs in patients with life-threatening COVID-19. Science 2020, 370, eabd4585. [Google Scholar] [CrossRef]
- Hamming, I.; Timens, W.; Bulthuis, M.L.; Lely, A.T.; Navis, G.; van Goor, H. Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis. J. Pathol. 2004, 203, 631–637. [Google Scholar] [CrossRef] [PubMed]
- Lee, J.S.; Shin, E.C. The type I interferon response in COVID-19: Implications for treatment. Nat. Rev. Immunol. 2020, 20, 585–586. [Google Scholar] [CrossRef] [PubMed]
- Wolfel, R.; Corman, V.M.; Guggemos, W.; Seilmaier, M.; Zange, S.; Muller, M.A.; Niemeyer, D.; Jones, T.C.; Vollmar, P.; Rothe, C.; et al. Virological assessment of hospitalized patients with COVID-2019. Nature 2020, 581, 465–469. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wilk, A.J.; Rustagi, A.; Zhao, N.Q.; Roque, J.; Martinez-Colon, G.J.; McKechnie, J.L.; Ivison, G.T.; Ranganath, T.; Vergara, R.; Hollis, T.; et al. A single-cell atlas of the peripheral immune response in patients with severe COVID-19. Nat. Med. 2020, 26, 1070–1076. [Google Scholar] [CrossRef] [PubMed]
- Zhou, Z.; Ren, L.; Zhang, L.; Zhong, J.; Xiao, Y.; Jia, Z.; Guo, L.; Yang, J.; Wang, C.; Jiang, S.; et al. Heightened Innate Immune Responses in the Respiratory Tract of COVID-19 Patients. Cell Host Microbe 2020, 27, 883–890.e2. [Google Scholar] [CrossRef]
- Channappanavar, R.; Perlman, S. Pathogenic human coronavirus infections: Causes and consequences of cytokine storm and immunopathology. Semin. Immunopathol. 2017, 39, 529–539. [Google Scholar] [CrossRef]
- Ye, Q.; Wang, B.; Mao, J. The pathogenesis and treatment of the `Cytokine Storm’ in COVID-19. J. Infect. 2020, 80, 607–613. [Google Scholar] [CrossRef]
- Zhao, J.; Zhao, J.; Perlman, S. T cell responses are required for protection from clinical disease and for virus clearance in severe acute respiratory syndrome coronavirus-infected mice. J. Virol. 2010, 84, 9318–9325. [Google Scholar] [CrossRef] [Green Version]
- Al-Samkari, H.; Karp Leaf, R.S.; Dzik, W.H.; Carlson, J.C.T.; Fogerty, A.E.; Waheed, A.; Goodarzi, K.; Bendapudi, P.K.; Bornikova, L.; Gupta, S.; et al. COVID-19 and coagulation: Bleeding and thrombotic manifestations of SARS-CoV-2 infection. Blood 2020, 136, 489–500. [Google Scholar] [CrossRef]
- Cao, W.; Li, T. COVID-19: Towards understanding of pathogenesis. Cell Res. 2020, 30, 367–369. [Google Scholar] [CrossRef]
- Ortega-Paz, L.; Capodanno, D.; Montalescot, G.; Angiolillo, D.J. Coronavirus Disease 2019-Associated Thrombosis and Coagulopathy: Review of the Pathophysiological Characteristics and Implications for Antithrombotic Management. J. Am. Heart Assoc. 2021, 10, e019650. [Google Scholar] [CrossRef] [PubMed]
- Ranucci, M.; Ballotta, A.; Di Dedda, U.; Bayshnikova, E.; Dei Poli, M.; Resta, M.; Falco, M.; Albano, G.; Menicanti, L. The procoagulant pattern of patients with COVID-19 acute respiratory distress syndrome. J. Thromb. Haemost. 2020, 18, 1747–1751. [Google Scholar] [CrossRef] [PubMed]
- Lee, A.Y.Y.; Connors, J.M.; Kreuziger, L.B.; Murphy, M.; Gernsheimer, T.; Lin, Y.; Huisman, M.; DeSancho, M. COVID-19 and Coagulopathy. Available online: https://www.hematology.org/covid-19/covid-19-and-coagulopathy (accessed on 1 November 2021).
- Connors, J.M.; Levy, J.H. COVID-19 and its implications for thrombosis and anticoagulation. Blood 2020, 135, 2033–2040. [Google Scholar] [CrossRef] [PubMed]
- Iba, T.; Levy, J.H. Sepsis-induced Coagulopathy and Disseminated Intravascular Coagulation. Anesthesiology 2020, 132, 1238–1245. [Google Scholar] [CrossRef]
- Panigada, M.; Bottino, N.; Tagliabue, P.; Grasselli, G.; Novembrino, C.; Chantarangkul, V.; Pesenti, A.; Peyvandi, F.; Tripodi, A. Hypercoagulability of COVID-19 patients in intensive care unit: A report of thromboelastography findings and other parameters of hemostasis. J. Thromb. Haemost. 2020, 18, 1738–1742. [Google Scholar] [CrossRef]
- Tang, N.; Bai, H.; Chen, X.; Gong, J.; Li, D.; Sun, Z. Anticoagulant treatment is associated with decreased mortality in severe coronavirus disease 2019 patients with coagulopathy. J. Thromb. Haemost. 2020, 18, 1094–1099. [Google Scholar] [CrossRef]
- Abou-Ismail, M.Y.; Diamond, A.; Kapoor, S.; Arafah, Y.; Nayak, L. The hypercoagulable state in COVID-19: Incidence, pathophysiology, and management. Thromb. Res. 2020, 194, 101–115. [Google Scholar] [CrossRef]
- Jackson, S.P.; Darbousset, R.; Schoenwaelder, S.M. Thromboinflammation: Challenges of therapeutically targeting coagulation and other host defense mechanisms. Blood 2019, 133, 906–918. [Google Scholar] [CrossRef] [Green Version]
- Kushner, A.; West, W.P.; Pillarisetty, L.S. Virchow Triad. In StatPearls; StatPearls Publishing: Treasure Island, FL, USA, 2021. [Google Scholar]
- Varga, Z.; Flammer, A.J.; Steiger, P.; Haberecker, M.; Andermatt, R.; Zinkernagel, A.S.; Mehra, M.R.; Schuepbach, R.A.; Ruschitzka, F.; Moch, H. Endothelial cell infection and endotheliitis in COVID-19. Lancet 2020, 395, 1417–1418. [Google Scholar] [CrossRef]
- Mehta, J.L.; Calcaterra, G.; Bassareo, P.P. COVID-19, thromboembolic risk, and Virchow’s triad: Lesson from the past. Clin. Cardiol. 2020, 43, 1362–1367. [Google Scholar] [CrossRef]
- Singhania, N.; Bansal, S.; Nimmatoori, D.P.; Ejaz, A.A.; McCullough, P.A.; Singhania, G. Current Overview on Hypercoagulability in COVID-19. Am. J. Cardiovasc. Drugs 2020, 20, 393–403. [Google Scholar] [CrossRef] [PubMed]
- Zuo, Y.; Yalavarthi, S.; Shi, H.; Gockman, K.; Zuo, M.; Madison, J.A.; Blair, C.; Weber, A.; Barnes, B.J.; Egeblad, M.; et al. Neutrophil extracellular traps in COVID-19. JCI Insight 2020, 5, e138999. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ahmed, S.; Zimba, O.; Gasparyan, A.Y. Thrombosis in Coronavirus disease 2019 (COVID-19) through the prism of Virchow’s triad. Clin. Rheumatol. 2020, 39, 2529–2543. [Google Scholar] [CrossRef] [PubMed]
- Guan, S.P.; Seet, R.C.S.; Kennedy, B.K. Does eNOS derived nitric oxide protect the young from severe COVID-19 complications? Ageing Res. Rev. 2020, 64, 101201. [Google Scholar] [CrossRef] [PubMed]
- Cernadas, M.R.; Sanchez de Miguel, L.; Garcia-Duran, M.; Gonzalez-Fernandez, F.; Millas, I.; Monton, M.; Rodrigo, J.; Rico, L.; Fernandez, P.; de Frutos, T.; et al. Expression of constitutive and inducible nitric oxide synthases in the vascular wall of young and aging rats. Circ. Res. 1998, 83, 279–286. [Google Scholar] [CrossRef] [Green Version]
- Bonetti, P.O.; Lerman, L.O.; Lerman, A. Endothelial dysfunction: A marker of atherosclerotic risk. Arterioscler. Thromb. Vasc. Biol. 2003, 23, 168–175. [Google Scholar] [CrossRef]
- Lotz, C.; Muellenbach, R.M.; Meybohm, P.; Mutlak, H.; Lepper, P.M.; Rolfes, C.B.; Peivandi, A.; Stumpner, J.; Kredel, M.; Kranke, P.; et al. Effects of inhaled nitric oxide in COVID-19-induced ARDS—Is it worthwhile? Acta Anaesthesiol. Scand. 2021, 65, 629–632. [Google Scholar] [CrossRef]
- Cooke, G.E.; Doshi, A.; Binkley, P.F. Endothelial nitric oxide synthase gene: Prospects for treatment of heart disease. Pharmacogenomics 2007, 8, 1723–1734. [Google Scholar] [CrossRef]
- Gao, Y.D.; Ding, M.; Dong, X.; Zhang, J.J.; Kursat Azkur, A.; Azkur, D.; Gan, H.; Sun, Y.L.; Fu, W.; Li, W.; et al. Risk factors for severe and critically ill COVID-19 patients: A review. Allergy 2021, 76, 428–455. [Google Scholar] [CrossRef]
- Long, L.; Zeng, X.; Zhang, X.; Xiao, W.; Guo, E.; Zhan, W.; Yang, X.; Li, C.; Wu, C.; Xu, T.; et al. Short-term outcomes of COVID-19 and risk factors for progression. Eur. Respir. J. 2020, 55, 2000990. [Google Scholar] [CrossRef] [Green Version]
- Cai, Q.; Huang, D.; Yu, H.; Zhu, Z.; Xia, Z.; Su, Y.; Li, Z.; Zhou, G.; Gou, J.; Qu, J.; et al. COVID-19: Abnormal liver function tests. J. Hepatol. 2020, 73, 566–574. [Google Scholar] [CrossRef] [PubMed]
- Kumar, A.; Kumar, P.; Dungdung, A.; Kumar Gupta, A.; Anurag, A.; Kumar, A. Pattern of liver function and clinical profile in COVID-19: A cross-sectional study of 91 patients. Diabetes Metab. Syndr. 2020, 14, 1951–1954. [Google Scholar] [CrossRef]
- Saini, R.K.; Saini, N.; Ram, S.; Soni, S.L.; Suri, V.; Malhotra, P.; Kaur, J.; Verma, I.; Sharma, S.; Zohmangaihi, D. COVID-19 associated variations in liver function parameters: A retrospective study. Postgrad. Med. J. 2020, 98, 91–97. [Google Scholar] [CrossRef] [PubMed]
- Ye, L.; Chen, B.; Wang, Y.; Yang, Y.; Zeng, J.; Deng, G.; Deng, Y.; Zeng, F. Prognostic value of liver biochemical parameters for COVID-19 mortality. Ann. Hepatol. 2021, 21, 100279. [Google Scholar] [CrossRef] [PubMed]
- Clark, R.; Waters, B.; Stanfill, A.G. Elevated liver function tests in COVID-19: Causes, clinical evidence, and potential treatments. Nurse Pract. 2021, 46, 21–26. [Google Scholar] [CrossRef] [PubMed]
- Kaushik, A.; Wani, S.N.; Baba, M.A.; Agarwal, A.K. Prevalence of Abnormal Liver Function Tests in COVID-19 Patients at a Tertiary Care Centre. J. Assoc. Physicians India 2020, 68, 73–75. [Google Scholar]
- Lv, Y.; Zhao, X.; Wang, Y.; Zhu, J.; Ma, C.; Feng, X.; Ma, Y.; Zheng, Y.; Yang, L.; Han, G.; et al. Abnormal Liver Function Tests Were Associated With Adverse Clinical Outcomes: An Observational Cohort Study of 2,912 Patients with COVID-19. Front. Med. 2021, 8, 639855. [Google Scholar] [CrossRef]
- Letko, M.; Marzi, A.; Munster, V. Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses. Nat. Microbiol. 2020, 5, 562–569. [Google Scholar] [CrossRef] [Green Version]
- Guo, H.F.; Vander Kooi, C.W. Neuropilin Functions as an Essential Cell Surface Receptor. J. Biol. Chem. 2015, 290, 29120–29126. [Google Scholar] [CrossRef] [Green Version]
- Plein, A.; Fantin, A.; Ruhrberg, C. Neuropilin regulation of angiogenesis, arteriogenesis, and vascular permeability. Microcirculation 2014, 21, 315–323. [Google Scholar] [CrossRef] [Green Version]
- Teesalu, T.; Sugahara, K.N.; Kotamraju, V.R.; Ruoslahti, E. C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration. Proc. Natl. Acad. Sci. USA 2009, 106, 16157–16162. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Cantuti-Castelvetri, L.; Ojha, R.; Pedro, L.D.; Djannatian, M.; Franz, J.; Kuivanen, S.; van der Meer, F.; Kallio, K.; Kaya, T.; Anastasina, M.; et al. Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity. Science 2020, 370, 856–860. [Google Scholar] [CrossRef] [PubMed]
- Kyrou, I.; Randeva, H.S.; Spandidos, D.A.; Karteris, E. Not only ACE2—The quest for additional host cell mediators of SARS-CoV-2 infection: Neuropilin-1 (NRP1) as a novel SARS-CoV-2 host cell entry mediator implicated in COVID-19. Signal Transduct. Target. Ther. 2021, 6, 21. [Google Scholar] [CrossRef] [PubMed]
- Mayi, B.S.; Leibowitz, J.A.; Woods, A.T.; Ammon, K.A.; Liu, A.E.; Raja, A. The role of Neuropilin-1 in COVID-19. PLoS Pathog. 2021, 17, e1009153. [Google Scholar] [CrossRef] [PubMed]
- Lukassen, S.; Chua, R.L.; Trefzer, T.; Kahn, N.C.; Schneider, M.A.; Muley, T.; Winter, H.; Meister, M.; Veith, C.; Boots, A.W.; et al. SARS-CoV-2 receptor ACE2 and TMPRSS2 are primarily expressed in bronchial transient secretory cells. EMBO J. 2020, 39, e105114. [Google Scholar] [CrossRef]
- Zhou, L.; Niu, Z.; Jiang, X.; Zhang, Z.; Zheng, Y.; Wang, Z.; Zhu, Y.; Gao, L.; Huang, H.; Wang, X.; et al. SARS-CoV-2 Targets by the pscRNA Profiling of ACE2, TMPRSS2 and Furin Proteases. iScience 2020, 23, 101744. [Google Scholar] [CrossRef]
- Millet, J.K.; Whittaker, G.R. Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells. Virology 2018, 517, 3–8. [Google Scholar] [CrossRef]
- Hulswit, R.J.; de Haan, C.A.; Bosch, B.J. Coronavirus Spike Protein and Tropism Changes. Adv. Virus Res. 2016, 96, 29–57. [Google Scholar] [CrossRef]
- Daly, J.L.; Simonetti, B.; Klein, K.; Chen, K.-E.; Williamson, M.K.; Antón-Plágaro, C.; Shoemark, D.K.; Simón-Gracia, L.; Bauer, M.; Hollandi, R.; et al. Neuropilin-1 is a host factor for SARS-CoV-2 infection. Science 2020, 370, 861–865. [Google Scholar] [CrossRef]
- Yeager, C.L.; Ashmun, R.A.; Williams, R.K.; Cardellichio, C.B.; Shapiro, L.H.; Look, A.T.; Holmes, K.V. Human aminopeptidase N is a receptor for human coronavirus 229E. Nature 1992, 357, 420–422. [Google Scholar] [CrossRef] [Green Version]
- Raj, V.S.; Mou, H.; Smits, S.L.; Dekkers, D.H.W.; Müller, M.A.; Dijkman, R.; Muth, D.; Demmers, J.A.A.; Zaki, A.; Fouchier, R.A.M.; et al. Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 2013, 495, 251–254. [Google Scholar] [CrossRef] [Green Version]
- Singh, M.; Bansal, V.; Feschotte, C. A Single-Cell RNA Expression Map of Human Coronavirus Entry Factors. Cell Rep. 2020, 32, 108175. [Google Scholar] [CrossRef] [PubMed]
- Schuler, B.A.; Habermann, A.C.; Plosa, E.J.; Taylor, C.J.; Jetter, C.; Negretti, N.M.; Kapp, M.E.; Benjamin, J.T.; Gulleman, P.; Nichols, D.S.; et al. Age-determined expression of priming protease TMPRSS2 and localization of SARS-CoV-2 in lung epithelium. J. Clin. Investig. 2021, 131, e140766. [Google Scholar] [CrossRef] [PubMed]
- Chow, R.D.; Majety, M.; Chen, S. The aging transcriptome and cellular landscape of the human lung in relation to SARS-CoV-2. Nat. Commun. 2021, 12, 4. [Google Scholar] [CrossRef] [PubMed]
- Ortiz, M.E.; Thurman, A.; Pezzulo, A.A.; Leidinger, M.R.; Klesney-Tait, J.A.; Karp, P.H.; Tan, P.; Wohlford-Lenane, C.; McCray, P.B., Jr.; Meyerholz, D.K. Heterogeneous expression of the SARS-Coronavirus-2 receptor ACE2 in the human respiratory tract. EBioMedicine 2020, 60, 102976. [Google Scholar] [CrossRef]
- Carrel, L.; Willard, H.F. X-inactivation profile reveals extensive variability in X-linked gene expression in females. Nature 2005, 434, 400–404. [Google Scholar] [CrossRef]
- V’kovski, P.; Gultom, M.; Steiner, S.; Kelly, J.; Russeil, J.; Mangeat, B.; Cora, E.; Pezoldt, J.; Holwerda, M.; Kratzel, A.; et al. Disparate temperature-dependent virus—Host dynamics for SARS-CoV-2 and SARS-CoV in the human respiratory epithelium. bioRxiv 2020. [Google Scholar] [CrossRef]
- Radzikowska, U.; Ding, M.; Tan, G.; Zhakparov, D.; Peng, Y.; Wawrzyniak, P.; Wang, M.; Li, S.; Morita, H.; Altunbulakli, C.; et al. Distribution of ACE2, CD147, CD26, and other SARS-CoV-2 associated molecules in tissues and immune cells in health and in asthma, COPD, obesity, hypertension, and COVID-19 risk factors. Allergy 2020, 75, 2829–2845. [Google Scholar] [CrossRef]
- Ziegler, C.G.K.; Allon, S.J.; Nyquist, S.K.; Mbano, I.M.; Miao, V.N.; Tzouanas, C.N.; Cao, Y.; Yousif, A.S.; Bals, J.; Hauser, B.M.; et al. SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues. Cell 2020, 181, 1016–1035.e19. [Google Scholar] [CrossRef]
- Li, Y.; Zhou, W.; Yang, L.; You, R. Physiological and pathological regulation of ACE2, the SARS-CoV-2 receptor. Pharmacol. Res. 2020, 157, 104833. [Google Scholar] [CrossRef]
- Zou, X.; Chen, K.; Zou, J.; Han, P.; Hao, J.; Han, Z. Single-cell RNA-seq data analysis on the receptor ACE2 expression reveals the potential risk of different human organs vulnerable to 2019-nCoV infection. Front. Med. 2020, 14, 185–192. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Salka, K.; Abutaleb, K.; Chorvinsky, E.; Thiruvengadam, G.; Arroyo, M.; Gomez, J.L.; Gutierrez, M.J.; Pillai, D.K.; Jaiswal, J.K.; Nino, G. IFN Stimulates ACE2 Expression in Pediatric Airway Epithelial Cells. Am. J. Respir. Cell Mol. Biol. 2021, 64, 515–518. [Google Scholar] [CrossRef] [PubMed]
- Scagnolari, C.; Bitossi, C.; Viscido, A.; Frasca, F.; Oliveto, G.; Scordio, M.; Petrarca, L.; Mancino, E.; Nenna, R.; Riva, E.; et al. ACE2 expression is related to the interferon response in airway epithelial cells but is that functional for SARS-CoV-2 entry? Cytokine 2021, 140, 155430. [Google Scholar] [CrossRef] [PubMed]
- Ni, W.; Yang, X.; Yang, D.; Bao, J.; Li, R.; Xiao, Y.; Hou, C.; Wang, H.; Liu, J.; Yang, D.; et al. Role of angiotensin-converting enzyme 2 (ACE2) in COVID-19. Crit. Care 2020, 24, 422. [Google Scholar] [CrossRef] [PubMed]
- Zhou, Z.; Yang, Z.; Ou, J.; Zhang, H.; Zhang, Q.; Dong, M.; Zhang, G. Temperature dependence of the SARS-CoV-2 affinity to human ACE2 determines COVID-19 progression and clinical outcome. Comput. Struct. Biotechnol. J. 2021, 19, 161–167. [Google Scholar] [CrossRef]
- Dai, Y.J.; Hu, F.; Li, H.; Huang, H.Y.; Wang, D.W.; Liang, Y. A profiling analysis on the receptor ACE2 expression reveals the potential risk of different type of cancers vulnerable to SARS-CoV-2 infection. Ann. Transl. Med. 2020, 8, 481. [Google Scholar] [CrossRef]
- Valdes, G.; Neves, L.A.; Anton, L.; Corthorn, J.; Chacon, C.; Germain, A.M.; Merrill, D.C.; Ferrario, C.M.; Sarao, R.; Penninger, J.; et al. Distribution of angiotensin-(1–7) and ACE2 in human placentas of normal and pathological pregnancies. Placenta 2006, 27, 200–207. [Google Scholar] [CrossRef]
- Kuba, K.; Imai, Y.; Rao, S.; Gao, H.; Guo, F.; Guan, B.; Huan, Y.; Yang, P.; Zhang, Y.; Deng, W.; et al. A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus-induced lung injury. Nat. Med. 2005, 11, 875–879. [Google Scholar] [CrossRef]
- Simoes e Silva, A.C.; Silveira, K.D.; Ferreira, A.J.; Teixeira, M.M. ACE2, angiotensin-(1–7) and Mas receptor axis in inflammation and fibrosis. Br. J. Pharmacol. 2013, 169, 477–492. [Google Scholar] [CrossRef] [Green Version]
- Jaimes, J.A.; Millet, J.K.; Whittaker, G.R. Proteolytic Cleavage of the SARS-CoV-2 Spike Protein and the Role of the Novel S1/S2 Site. iScience 2020, 23, 101212. [Google Scholar] [CrossRef]
- Papageorgiou, A.C.; Mohsin, I. The SARS-CoV-2 Spike Glycoprotein as a Drug and Vaccine Target: Structural Insights into Its Complexes with ACE2 and Antibodies. Cells 2020, 9, 2343. [Google Scholar] [CrossRef] [PubMed]
- Benton, D.J.; Wrobel, A.G.; Xu, P.; Roustan, C.; Martin, S.R.; Rosenthal, P.B.; Skehel, J.J.; Gamblin, S.J. Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion. Nature 2020, 588, 327–330. [Google Scholar] [CrossRef] [PubMed]
- Wang, M.Y.; Zhao, R.; Gao, L.J.; Gao, X.F.; Wang, D.P.; Cao, J.M. SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development. Front. Cell. Infect. Microbiol. 2020, 10, 587269. [Google Scholar] [CrossRef] [PubMed]
- Yang, J.; Petitjean, S.J.L.; Koehler, M.; Zhang, Q.; Dumitru, A.C.; Chen, W.; Derclaye, S.; Vincent, S.P.; Soumillion, P.; Alsteens, D. Molecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor. Nat. Commun. 2020, 11, 4541. [Google Scholar] [CrossRef]
- Walls, A.C.; Park, Y.J.; Tortorici, M.A.; Wall, A.; McGuire, A.T.; Veesler, D. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell 2020, 181, 281–292.e6. [Google Scholar] [CrossRef]
- Casalino, L.; Gaieb, Z.; Goldsmith, J.A.; Hjorth, C.K.; Dommer, A.C.; Harbison, A.M.; Fogarty, C.A.; Barros, E.P.; Taylor, B.C.; McLellan, J.S.; et al. Beyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein. ACS Cent. Sci. 2020, 6, 1722–1734. [Google Scholar] [CrossRef]
- Toelzer, C.; Gupta, K.; Yadav, S.K.N.; Borucu, U.; Davidson, A.D.; Kavanagh Williamson, M.; Shoemark, D.K.; Garzoni, F.; Staufer, O.; Milligan, R.; et al. Free fatty acid binding pocket in the locked structure of SARS-CoV-2 spike protein. Science 2020, 370, 725–730. [Google Scholar] [CrossRef]
- Dan, J.M.; Mateus, J.; Kato, Y.; Hastie, K.M.; Yu, E.D.; Faliti, C.E.; Grifoni, A.; Ramirez, S.I.; Haupt, S.; Frazier, A.; et al. Immunological memory to SARS-CoV-2 assessed for up to 8 months after infection. Science 2021, 371, eabf4063. [Google Scholar] [CrossRef]
- Figueiredo-Campos, P.; Blankenhaus, B.; Mota, C.; Gomes, A.; Serrano, M.; Ariotti, S.; Costa, C.; Nunes-Cabaco, H.; Mendes, A.M.; Gaspar, P.; et al. Seroprevalence of anti-SARS-CoV-2 antibodies in COVID-19 patients and healthy volunteers up to 6 months post disease onset. Eur. J. Immunol. 2020, 50, 2025–2040. [Google Scholar] [CrossRef]
- Gaebler, C.; Wang, Z.; Lorenzi, J.C.C.; Muecksch, F.; Finkin, S.; Tokuyama, M.; Cho, A.; Jankovic, M.; Schaefer-Babajew, D.; Oliveira, T.Y.; et al. Evolution of antibody immunity to SARS-CoV-2. Nature 2021, 591, 639–644. [Google Scholar] [CrossRef]
- Chan, J.F.; Kok, K.H.; Zhu, Z.; Chu, H.; To, K.K.; Yuan, S.; Yuen, K.Y. Genomic characterization of the 2019 novel human-pathogenic coronavirus isolated from a patient with atypical pneumonia after visiting Wuhan. Emerg. Microbes Infect. 2020, 9, 221–236. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hachim, A.; Kavian, N.; Cohen, C.A.; Chin, A.W.H.; Chu, D.K.W.; Mok, C.K.P.; Tsang, O.T.Y.; Yeung, Y.C.; Perera, R.; Poon, L.L.M.; et al. ORF8 and ORF3b antibodies are accurate serological markers of early and late SARS-CoV-2 infection. Nat. Immunol. 2020, 21, 1293–1301. [Google Scholar] [CrossRef] [PubMed]
- Wajnberg, A.; Amanat, F.; Firpo, A.; Altman, D.R.; Bailey, M.J.; Mansour, M.; McMahon, M.; Meade, P.; Mendu, D.R.; Muellers, K.; et al. SARS-CoV-2 infection induces robust, neutralizing antibody responses that are stable for at least three months. medRxiv 2020. [Google Scholar] [CrossRef]
- Rodda, L.B.; Netland, J.; Shehata, L.; Pruner, K.B.; Morawski, P.A.; Thouvenel, C.D.; Takehara, K.K.; Eggenberger, J.; Hemann, E.A.; Waterman, H.R.; et al. Functional SARS-CoV-2-Specific Immune Memory Persists after Mild COVID-19. Cell 2021, 184, 169–183.e17. [Google Scholar] [CrossRef] [PubMed]
- Amirlak, L.; Haddad, R.; Hardy, J.D.; Khaled, N.S.; Chung, M.H.; Amirlak, B. Effectiveness of booster BCG vaccination in preventing Covid-19 infection. Hum. Vaccines Immunother. 2021, 17, 3913–3915. [Google Scholar] [CrossRef] [PubMed]
- Braun, J.; Loyal, L.; Frentsch, M.; Wendisch, D.; Georg, P.; Kurth, F.; Hippenstiel, S.; Dingeldey, M.; Kruse, B.; Fauchere, F.; et al. SARS-CoV-2-reactive T cells in healthy donors and patients with COVID-19. Nature 2020, 587, 270–274. [Google Scholar] [CrossRef] [PubMed]
- Klinger, D.; Blass, I.; Rappoport, N.; Linial, M. Significantly Improved COVID-19 Outcomes in Countries with Higher BCG Vaccination Coverage: A Multivariable Analysis. Vaccines 2020, 8, 378. [Google Scholar] [CrossRef]
- Le Bert, N.; Tan, A.T.; Kunasegaran, K.; Tham, C.Y.L.; Hafezi, M.; Chia, A.; Chng, M.H.Y.; Lin, M.; Tan, N.; Linster, M.; et al. SARS-CoV-2-specific T cell immunity in cases of COVID-19 and SARS, and uninfected controls. Nature 2020, 584, 457–462. [Google Scholar] [CrossRef]
- Mateus, J.; Grifoni, A.; Tarke, A.; Sidney, J.; Ramirez, S.I.; Dan, J.M.; Burger, Z.C.; Rawlings, S.A.; Smith, D.M.; Phillips, E.; et al. Selective and cross-reactive SARS-CoV-2 T cell epitopes in unexposed humans. Science 2020, 370, 89–94. [Google Scholar] [CrossRef]
- Netea, M.G.; Quintin, J.; van der Meer, J.W. Trained immunity: A memory for innate host defense. Cell Host Microbe 2011, 9, 355–361. [Google Scholar] [CrossRef] [Green Version]
- Green, S.J.; Nacy, C.A.; Schreiber, R.D.; Granger, D.L.; Crawford, R.M.; Meltzer, M.S.; Fortier, A.H. Neutralization of gamma interferon and tumor necrosis factor alpha blocks in vivo synthesis of nitrogen oxides from L-arginine and protection against Francisella tularensis infection in Mycobacterium bovis BCG-treated mice. Infect. Immun. 1993, 61, 689–698. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Mantovani, A.; Netea, M.G. Trained Innate Immunity, Epigenetics, and Covid-19. N. Engl. J. Med. 2020, 383, 1078–1080. [Google Scholar] [CrossRef] [PubMed]
- To, K.K.; Hung, I.F.; Ip, J.D.; Chu, A.W.; Chan, W.M.; Tam, A.R.; Fong, C.H.; Yuan, S.; Tsoi, H.W.; Ng, A.C.; et al. COVID-19 re-infection by a phylogenetically distinct SARS-coronavirus-2 strain confirmed by whole genome sequencing. Clin. Infect. Dis. 2020, 73, e2946–e2951. [Google Scholar] [CrossRef] [PubMed]
- Harvey, R.A.; Rassen, J.A.; Kabelac, C.A.; Turenne, W.; Leonard, S.; Klesh, R.; Meyer, W.A.; Kaufman, H.W.; Anderson, S.; Cohen, O.; et al. Real-world data suggest antibody positivity to SARS-CoV-2 is associated with a decreased risk of future infection. medRxiv 2020. [Google Scholar] [CrossRef]
- Lumley, S.F.; O’Donnell, D.; Stoesser, N.E.; Matthews, P.C.; Howarth, A.; Hatch, S.B.; Marsden, B.D.; Cox, S.; James, T.; Warren, F.; et al. Antibody Status and Incidence of SARS-CoV-2 Infection in Health Care Workers. N. Engl. J. Med. 2021, 384, 533–540. [Google Scholar] [CrossRef]
- McMahan, K.; Yu, J.; Mercado, N.B.; Loos, C.; Tostanoski, L.H.; Chandrashekar, A.; Liu, J.; Peter, L.; Atyeo, C.; Zhu, A.; et al. Correlates of protection against SARS-CoV-2 in rhesus macaques. Nature 2021, 590, 630–634. [Google Scholar] [CrossRef] [PubMed]
- Wise, J. Covid-19: New coronavirus variant is identified in UK. BMJ 2020, 371, m4857. [Google Scholar] [CrossRef]
- Davies, N.G.; Abbott, S.; Barnard, R.C.; Jarvis, C.I.; Kucharski, A.J.; Munday, J.D.; Pearson, C.A.B.; Russell, T.W.; Tully, D.C.; Washburne, A.D.; et al. Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England. Science 2021, 372, eabg3055. [Google Scholar] [CrossRef]
- Tegally, H.; Wilkinson, E.; Giovanetti, M.; Iranzadeh, A.; Fonseca, V.; Giandhari, J.; Doolabh, D.; Pillay, S.; San, E.J.; Msomi, N.; et al. Detection of a SARS-CoV-2 variant of concern in South Africa. Nature 2021, 592, 438–443. [Google Scholar] [CrossRef]
- Faria, N.R.; Mellan, T.A.; Whittaker, C.; Claro, I.M.; Candido, D.D.S.; Mishra, S.; Crispim, M.A.E.; Sales, F.C.S.; Hawryluk, I.; McCrone, J.T.; et al. Genomics and epidemiology of the P.1 SARS-CoV-2 lineage in Manaus, Brazil. Science 2021, 372, 815–821. [Google Scholar] [CrossRef]
- Zhang, J.; Xiao, T.; Cai, Y.; Lavine, C.L.; Peng, H.; Zhu, H.; Anand, K.; Tong, P.; Gautam, A.; Mayer, M.L.; et al. Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant. Science 2021, 374, 1353–1360. [Google Scholar] [CrossRef] [PubMed]
- Mlcochova, P.; Kemp, S.; Dhar, M.S.; Papa, G.; Meng, B.; Ferreira, I.; Datir, R.; Collier, D.A.; Albecka, A.; Singh, S.; et al. SARS-CoV-2 B.1.617.2 Delta variant replication and immune evasion. Nature 2021, 599, 114–119. [Google Scholar] [CrossRef] [PubMed]
- (CDC), Centers for Disease Control and Prevention. SARS-CoV-2 Variant Classifications and Definitions. Available online: https://www.cdc.gov/coronavirus/2019-ncov/variants/variant-info.html (accessed on 22 September 2021).
- Korber, B.; Fischer, W.M.; Gnanakaran, S.; Yoon, H.; Theiler, J.; Abfalterer, W.; Hengartner, N.; Giorgi, E.E.; Bhattacharya, T.; Foley, B.; et al. Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus. Cell 2020, 182, 812–827.e19. [Google Scholar] [CrossRef] [PubMed]
- Plante, J.A.; Liu, Y.; Liu, J.; Xia, H.; Johnson, B.A.; Lokugamage, K.G.; Zhang, X.; Muruato, A.E.; Zou, J.; Fontes-Garfias, C.R.; et al. Spike mutation D614G alters SARS-CoV-2 fitness. Nature 2021, 592, 116–121. [Google Scholar] [CrossRef]
- Zhang, L.; Jackson, C.B.; Mou, H.; Ojha, A.; Peng, H.; Quinlan, B.D.; Rangarajan, E.S.; Pan, A.; Vanderheiden, A.; Suthar, M.S.; et al. SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity. Nat. Commun. 2020, 11, 6013. [Google Scholar] [CrossRef]
- Butowt, R.; Bilinska, K.; Von Bartheld, C.S. Chemosensory Dysfunction in COVID-19: Integration of Genetic and Epidemiological Data Points to D614G Spike Protein Variant as a Contributing Factor. ACS Chem. Neurosci. 2020, 11, 3180–3184. [Google Scholar] [CrossRef]
- Yurkovetskiy, L.; Wang, X.; Pascal, K.E.; Tomkins-Tinch, C.; Nyalile, T.P.; Wang, Y.; Baum, A.; Diehl, W.E.; Dauphin, A.; Carbone, C.; et al. Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant. Cell 2020, 183, 739–751.e8. [Google Scholar] [CrossRef]
- Zhou, B.; Thao, T.T.N.; Hoffmann, D.; Taddeo, A.; Ebert, N.; Labroussaa, F.; Pohlmann, A.; King, J.; Steiner, S.; Kelly, J.N.; et al. SARS-CoV-2 spike D614G change enhances replication and transmission. Nature 2021, 592, 122–127. [Google Scholar] [CrossRef]
- Gobeil, S.M.; Janowska, K.; McDowell, S.; Mansouri, K.; Parks, R.; Manne, K.; Stalls, V.; Kopp, M.F.; Henderson, R.; Edwards, R.J.; et al. D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction. Cell Rep. 2021, 34, 108630. [Google Scholar] [CrossRef]
- Daniloski, Z.; Jordan, T.X.; Ilmain, J.K.; Guo, X.; Bhabha, G.; tenOever, B.R.; Sanjana, N.E. The Spike D614G mutation increases SARS-CoV-2 infection of multiple human cell types. eLife 2021, 10, e65365. [Google Scholar] [CrossRef] [PubMed]
- Lan, J.; Ge, J.; Yu, J.; Shan, S.; Zhou, H.; Fan, S.; Zhang, Q.; Shi, X.; Wang, Q.; Zhang, L.; et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature 2020, 581, 215–220. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Liu, H.; Zhang, Q.; Wei, P.; Chen, Z.; Aviszus, K.; Yang, J.; Downing, W.; Jiang, C.; Liang, B.; Reynoso, L.; et al. The basis of a more contagious 501Y.V1 variant of SARS-CoV-2. Cell Res. 2021, 31, 720–722. [Google Scholar] [CrossRef] [PubMed]
- Socher, E.; Conrad, M.; Heger, L.; Paulsen, F.; Sticht, H.; Zunke, F.; Arnold, P. Computational decomposition reveals reshaping of the SARS-CoV-2–ACE2 interface among viral variants expressing the N501Y mutation. J. Cell. Biochem. 2021, 122, 1863–1872. [Google Scholar] [CrossRef]
- Zhu, X.; Mannar, D.; Srivastava, S.S.; Berezuk, A.M.; Demers, J.P.; Saville, J.W.; Leopold, K.; Li, W.; Dimitrov, D.S.; Tuttle, K.S.; et al. Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies. PLoS Biol. 2021, 19, e3001237. [Google Scholar] [CrossRef] [PubMed]
- Tian, F.; Tong, B.; Sun, L.; Shi, S.; Zheng, B.; Wang, Z.; Dong, X.; Zheng, P. N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding to receptor ACE2. eLife 2021, 10, e69091. [Google Scholar] [CrossRef] [PubMed]
- Ostrov, D.A. Structural Consequences of Variation in SARS-CoV-2 B.1.1.7. J. Cell. Immunol. 2021, 3, 103–108. [Google Scholar] [CrossRef] [PubMed]
- Peacock, T.P.; Goldhill, D.H.; Zhou, J.; Baillon, L.; Frise, R.; Swann, O.C.; Kugathasan, R.; Penn, R.; Brown, J.C.; Sanchez-David, R.Y.; et al. The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets. Nat. Microbiol. 2021, 6, 899–909. [Google Scholar] [CrossRef]
- Mohammad, A.; Abubaker, J.; Al-Mulla, F. Structural modelling of SARS-CoV-2 alpha variant (B.1.1.7) suggests enhanced furin binding and infectivity. Virus Res. 2021, 303, 198522. [Google Scholar] [CrossRef]
- Lubinski, B.; Fernandes, M.H.V.; Frazier, L.; Tang, T.; Daniel, S.; Diel, D.G.; Jaimes, J.A.; Whittaker, G.R. Functional evaluation of the P681H mutation on the proteolytic activation of the SARS-CoV-2 variant B.1.1.7 (Alpha) spike. iScience 2022, 25, 103589. [Google Scholar] [CrossRef]
- Liu, H.; Wei, P.; Zhang, Q.; Chen, Z.; Aviszus, K.; Downing, W.; Peterson, S.; Reynoso, L.; Downey, G.P.; Frankel, S.K.; et al. 501Y.V2 and 501Y.V3 variants of SARS-CoV-2 lose binding to bamlanivimab in vitro. mAbs 2021, 13, 1919285. [Google Scholar] [CrossRef]
- Kim, S.; Liu, Y.; Lei, Z.; Dicker, J.; Cao, Y.; Zhang, X.F.; Im, W. Differential Interactions Between Human ACE2 and Spike RBD of SARS-CoV-2 Variants of Concern. bioRxiv 2021. [Google Scholar] [CrossRef] [PubMed]
- Planas, D.; Bruel, T.; Grzelak, L.; Guivel-Benhassine, F.; Staropoli, I.; Porrot, F.; Planchais, C.; Buchrieser, J.; Rajah, M.M.; Bishop, E.; et al. Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies. Nat. Med. 2021, 27, 917–924. [Google Scholar] [CrossRef] [PubMed]
- Arora, P.; Sidarovich, A.; Kruger, N.; Kempf, A.; Nehlmeier, I.; Graichen, L.; Moldenhauer, A.S.; Winkler, M.S.; Schulz, S.; Jack, H.M.; et al. B.1.617.2 enters and fuses lung cells with increased efficiency and evades antibodies induced by infection and vaccination. Cell Rep. 2021, 37, 109825. [Google Scholar] [CrossRef] [PubMed]
- Jalkanen, P.; Kolehmainen, P.; Hakkinen, H.K.; Huttunen, M.; Tahtinen, P.A.; Lundberg, R.; Maljanen, S.; Reinholm, A.; Tauriainen, S.; Pakkanen, S.H.; et al. COVID-19 mRNA vaccine induced antibody responses against three SARS-CoV-2 variants. Nat. Commun. 2021, 12, 3991. [Google Scholar] [CrossRef]
- Wang, Z.; Schmidt, F.; Weisblum, Y.; Muecksch, F.; Barnes, C.O.; Finkin, S.; Schaefer-Babajew, D.; Cipolla, M.; Gaebler, C.; Lieberman, J.A.; et al. mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants. Nature 2021, 592, 616–622. [Google Scholar] [CrossRef]
- Greaney, A.J.; Loes, A.N.; Crawford, K.H.D.; Starr, T.N.; Malone, K.D.; Chu, H.Y.; Bloom, J.D. Comprehensive mapping of mutations in the SARS-CoV-2 receptor-binding domain that affect recognition by polyclonal human plasma antibodies. Cell Host Microbe 2021, 29, 463–476.e6. [Google Scholar] [CrossRef]
- Zhang, J.; Xiao, T.; Cai, Y.; Lavine, C.L.; Peng, H.; Zhu, H.; Anand, K.; Tong, P.; Gautam, A.; Mayer, M.L.; et al. Membrane fusion and immune evasion by the spike protein of SARS-CoV-2 Delta variant. bioRxiv 2021. [Google Scholar] [CrossRef]
- Starr, T.N.; Greaney, A.J.; Dingens, A.S.; Bloom, J.D. Complete map of SARS-CoV-2 RBD mutations that escape the monoclonal antibody LY-CoV555 and its cocktail with LY-CoV016. Cell Rep. Med. 2021, 2, 100255. [Google Scholar] [CrossRef]
- Geers, D.; Shamier, M.C.; Bogers, S.; den Hartog, G.; Gommers, L.; Nieuwkoop, N.N.; Schmitz, K.S.; Rijsbergen, L.C.; van Osch, J.A.T.; Dijkhuizen, E.; et al. SARS-CoV-2 variants of concern partially escape humoral but not T-cell responses in COVID-19 convalescent donors and vaccinees. Sci. Immunol. 2021, 6, eabj1750. [Google Scholar] [CrossRef]
- Hall, V.G.; Ferreira, V.H.; Wood, H.; Ierullo, M.; Majchrzak-Kita, B.; Manguiat, K.; Robinson, A.; Kulasingam, V.; Humar, A.; Kumar, D. Delayed-interval BNT162b2 mRNA COVID-19 vaccination enhances humoral immunity and induces robust T cell responses. Nat. Immunol. 2022, 23, 380–385. [Google Scholar] [CrossRef]
- Riou, C.; Keeton, R.; Moyo-Gwete, T.; Hermanus, T.; Kgagudi, P.; Baguma, R.; Valley-Omar, Z.; Smith, M.; Tegally, H.; Doolabh, D.; et al. Escape from recognition of SARS-CoV-2 variant spike epitopes but overall preservation of T cell immunity. Sci. Transl. Med. 2022, 14, eabj6824. [Google Scholar] [CrossRef] [PubMed]
- Goel, R.R.; Painter, M.M.; Apostolidis, S.A.; Mathew, D.; Meng, W.; Rosenfeld, A.M.; Lundgreen, K.A.; Reynaldi, A.; Khoury, D.S.; Pattekar, A.; et al. mRNA vaccines induce durable immune memory to SARS-CoV-2 and variants of concern. Science 2021, 374, abm0829. [Google Scholar] [CrossRef] [PubMed]
- Woldemeskel, B.A.; Garliss, C.C.; Blankson, J.N. mRNA Vaccine-Elicited SARS-CoV-2-Specific T cells Persist at 6 Months and Recognize the Delta Variant. Clin. Infect. Dis. 2021, ciab915. [Google Scholar] [CrossRef] [PubMed]
- Jordan, S.C.; Shin, B.H.; Gadsden, T.M.; Chu, M.; Petrosyan, A.; Le, C.N.; Zabner, R.; Oft, J.; Pedraza, I.; Cheng, S.; et al. T cell immune responses to SARS-CoV-2 and variants of concern (Alpha and Delta) in infected and vaccinated individuals. Cell. Mol. Immunol. 2021, 18, 2554–2556. [Google Scholar] [CrossRef] [PubMed]
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. |
© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Share and Cite
Fayyad, D.; Kelts, J.L.; Nielson, T.H.; Epelle, I.L.; Monear, N.C.; Strawn, M.T.G.; Woerner, B.N.; Xhabija, B. COVID-19: A Systematic Review of the Transmissibility, Pathogenesis, Entry Factors, and Signature Immune Response. BioChem 2022, 2, 115-144. https://doi.org/10.3390/biochem2020009
Fayyad D, Kelts JL, Nielson TH, Epelle IL, Monear NC, Strawn MTG, Woerner BN, Xhabija B. COVID-19: A Systematic Review of the Transmissibility, Pathogenesis, Entry Factors, and Signature Immune Response. BioChem. 2022; 2(2):115-144. https://doi.org/10.3390/biochem2020009
Chicago/Turabian StyleFayyad, Deena, Jessica L. Kelts, Tristan H. Nielson, Ibiere Lovelyn Epelle, Nicodemus C. Monear, Miguel T. G. Strawn, Benjamin N. Woerner, and Besa Xhabija. 2022. "COVID-19: A Systematic Review of the Transmissibility, Pathogenesis, Entry Factors, and Signature Immune Response" BioChem 2, no. 2: 115-144. https://doi.org/10.3390/biochem2020009
APA StyleFayyad, D., Kelts, J. L., Nielson, T. H., Epelle, I. L., Monear, N. C., Strawn, M. T. G., Woerner, B. N., & Xhabija, B. (2022). COVID-19: A Systematic Review of the Transmissibility, Pathogenesis, Entry Factors, and Signature Immune Response. BioChem, 2(2), 115-144. https://doi.org/10.3390/biochem2020009