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Antiviral Activity of Lectins
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Antiviral Activity of Lectins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pharmacology".

Deadline for manuscript submissions: closed (20 October 2024) | Viewed by 3687

Special Issue Editor

Dr. Yuichiro Sato

E-Mail Website
Guest Editor
Department of Medical Pharmacy, Faculty of Pharmacy, Yasuda Women’s University, 6-13-1 Yasuhigashi, Asaminami, Hiroshima 731-0153, Japan
Interests: lectin; antiviral activity; anticancer activity; autophagy; anti-influenza virus activity
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Lectins are ubiquitous proteins found in various taxonomy, animals, plants, algae, and bacteria. Numerous lectins have been reported to show antiviral activity against viruses such as influenza virus, human immunodeficiency virus (HIV), SARS-CoV, ebola virus, human herpes viruses, and hepatitis C virus (HCV). As the glycan profiles on viral surface are diverse among these viruses, antiviral potency of lectins are largely depended on their unique carbohydrate-binding specificity as well as the characteristic structure of lectins. Like the pandemic case caused by the recent emerged SARS-CoV-2, we are consistently facing the risk to encounter unknown viruses to which no one has sufficient immunity. Therefore, antiviral agents are in great demand to confront the emergence of new viruses. To develop therapeutic or prophylactic agents targeted for pathogenic viral glycans, fundamental information on lectin-virus interaction via glycan moiety is truly valuable. In this open-access special issue, we welcome any research articles regarding novel aspects of antiviral lectins. We hope that this issue will contribute to advancing our understanding on lectins that are ultimately applicable for microbicides to prevent the transmission of viruses.

Dr. Yuichiro Sato
Guest Editor

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Keywords

  • lectin
  • carbohydrate-binding specificity
  • virus
  • antiviral activity
  • glycan

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Published Papers (2 papers)

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Research

17 pages, 2497 KiB  
Article
Microcystis viridis NIES-102 Cyanobacteria Lectin (MVL) Interacts with SARS-CoV-2 Spike Protein Receptor Binding Domains (RBDs) via Protein–Protein Interaction
by Zhengguang Wang, Zhihan Yang, Mami Shishido, Khadija Daoudi, Masafumi Hidaka, Hiroaki Tateno, Eugene Futai and Tomohisa Ogawa
Int. J. Mol. Sci. 2024, 25(12), 6696; https://doi.org/10.3390/ijms25126696 - 18 Jun 2024
Cited by 1 | Viewed by 1489
Abstract
The emergence of coronavirus disease 2019 (COVID-19) posed a major challenge to healthcare systems worldwide, especially as mutations in the culprit Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) complicated the development of vaccines and antiviral drugs. Therefore, the search for natural products with [...] Read more.
The emergence of coronavirus disease 2019 (COVID-19) posed a major challenge to healthcare systems worldwide, especially as mutations in the culprit Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) complicated the development of vaccines and antiviral drugs. Therefore, the search for natural products with broad anti-SARS-CoV-2 capabilities is an important option for the prevention and treatment of similar infectious diseases. Lectins, which are widely recognized as antiviral agents, could contribute to the development of anti-SARS-CoV-2 drugs. This study evaluated the binding affinity of six lectins (including the cyanobacterial lectin from Microcystis viridis NIES-102 (MVL), and Jacalin, a lectin from the breadfruit, Artocarpus altilis) to the receptor binding domain (RBD) of the spike protein on the original (wild) SARS-CoV-2 and three of its mutants: Alpha, Delta, and Omicron. MVL and Jacalin showed distinct binding affinity to the RBDs of the four SARS-CoV-2 strains. The remaining four lectins (DB1, ConA, PHA-M and CSL3) showed no such binding affinity. Although the glycan specificities of MVL and Jacalin were different, they showed the same affinity for the spike protein RBDs of the four SARS-CoV-2 strains, in the order of effectiveness Alpha > Delta > original > Omicron. The verification of glycan-specific inhibition revealed that both lectins bind to RBDs by glycan-specific recognition, but, in addition, MVL binds to RBDs through protein–protein interactions. Full article
(This article belongs to the Special Issue Antiviral Activity of Lectins)
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14 pages, 2386 KiB  
Article
A Complex-Type N-Glycan-Specific Lectin Isolated from Green Alga Halimeda borneensis Exhibits Potent Anti-Influenza Virus Activity
by Jinmin Mu, Makoto Hirayama, Kinjiro Morimoto and Kanji Hori
Int. J. Mol. Sci. 2024, 25(8), 4345; https://doi.org/10.3390/ijms25084345 - 15 Apr 2024
Cited by 1 | Viewed by 1478
Abstract
Marine algal lectins specific for high-mannose N-glycans have attracted attention because they strongly inhibit the entry of enveloped viruses, including influenza viruses and SARS-CoV-2, into host cells by binding to high-mannose-type N-glycans on viral surfaces. Here, we report a novel anti-influenza [...] Read more.
Marine algal lectins specific for high-mannose N-glycans have attracted attention because they strongly inhibit the entry of enveloped viruses, including influenza viruses and SARS-CoV-2, into host cells by binding to high-mannose-type N-glycans on viral surfaces. Here, we report a novel anti-influenza virus lectin (named HBL40), specific for complex-type N-glycans, which was isolated from a marine green alga, Halimeda borneensis. The hemagglutination activity of HBL40 was inhibited with both complex-type N-glycan and O-glycan-linked glycoproteins but not with high-mannose-type N-glycan-linked glycoproteins or any of the monosaccharides examined. In the oligosaccharide-binding experiment using 26 pyridylaminated oligosaccharides, HBL40 only bound to complex-type N-glycans with bi- and triantennary-branched sugar chains. The sialylation, core fucosylation, and the increased number of branched antennae of the N-glycans lowered the binding activity with HBL40. Interestingly, the lectin potently inhibited the infection of influenza virus (A/H3N2/Udorn/72) into NCI-H292 cells at IC50 of 8.02 nM by binding to glycosylated viral hemagglutinin (KD of 1.21 × 10−6 M). HBL40 consisted of two isolectins with slightly different molecular masses to each other that could be separated by reverse-phase HPLC. Both isolectins shared the same 16 N-terminal amino acid sequences. Thus, HBL40 could be useful as an antivirus lectin specific for complex-type N-glycans. Full article
(This article belongs to the Special Issue Antiviral Activity of Lectins)
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