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Viruses
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Glycans in Virus-Host Interactions
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Glycans in Virus-Host Interactions

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Animal Viruses".

Deadline for manuscript submissions: 15 July 2025 | Viewed by 13509

Special Issue Editor

Dr. Rahul Raman

E-Mail Website
Guest Editor
Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA
Interests: stuctural biology; computational biology; structure–function relationships of glycan–protein interactions; engineering and development of glycoprotein and antibody-based therapeutics

Special Issue Information

Dear Colleagues,

Glycosylation is a common post-translational modification of all proteins. Consequently, complex glycans are displayed on the surfaces of viruses, and host tissues and cells, with multidimensional roles in pathogen–host interactions. Attachment of viruses to cell surface receptors is the initial step in infection. Many mammalian viruses have evolved to recognize receptors that are glycans on cell surface glycoproteins or glycolipids. Viral surface glycans shield vulnerable protein epitopes from host immunity, but can also present distinct "glycoepitopes" that can be targeted as novel antigens for therapeutic response to infectious diseases. This Special Issue focuses on articles that cover the following areas: (1) characterization of glycosylation in the context of viral surface glycoproteins and glycan receptors displayed on specific host cells or tissues infected by a virus; (2) characterization of the sequence and structural specificity of recognition of glycan receptors by viruses and/or viral proteins; (3) the design and engineering of novel therapeutic agents, such as antibodies, that recognize distinct glycoepitopes on viral surfaces and achieve potent neutralization or other glycan-binding proteins (including lectins) that can specifically block interactions involving virus and host receptors.

Dr. Rahul Raman
Guest Editor

Manuscript Submission Information

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • glycoeptiope
  • glycan receptors
  • viruses
  • antibodies
  • lectins

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Published Papers (4 papers)

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Research

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14 pages, 3265 KiB  
Article
Identification of Three Novel O-Linked Glycans in the Envelope Protein of Tick-Borne Encephalitis Virus
by Ebba Könighofer, Ekaterina Mirgorodskaya, Kristina Nyström, Karin Stiasny, Ambjörn Kärmander, Tomas Bergström and Rickard Nordén
Viruses 2024, 16(12), 1891; https://doi.org/10.3390/v16121891 - 8 Dec 2024
Viewed by 1137
Abstract
The tick-borne encephalitis virus is a pathogen endemic to northern Europe and Asia, transmitted through bites from infected ticks. It is a member of the Flaviviridae family and possesses a positive-sense, single-stranded RNA genome encoding a polypeptide that is processed into seven non-structural [...] Read more.
The tick-borne encephalitis virus is a pathogen endemic to northern Europe and Asia, transmitted through bites from infected ticks. It is a member of the Flaviviridae family and possesses a positive-sense, single-stranded RNA genome encoding a polypeptide that is processed into seven non-structural and three structural proteins, including the envelope (E) protein. The glycosylation of the E protein, involving a single N-linked glycan at position N154, plays a critical role in viral infectivity and pathogenesis. Here, we dissected the entire glycosylation profile of the E protein using liquid chromatography-tandem mass spectrometry and identified three novel O-linked glycans, which were found at relatively low frequency. One of the O-linked glycans was positioned close to the highly conserved N-linked glycan site, and structural analysis suggested that it may be relevant for the function of the E 150-loop. The N154 site was found to be glycosylated with a high frequency, containing oligomannose or complex-type structures, some of which were fucosylated. An unusually high portion of oligomannose N-linked glycan structures exhibited compositions that are normally observed on proteins when they are translocated from the endoplasmic reticulum to the trans-Golgi network, suggesting disruption of the glycan processing pathway in the infected cells from which the E protein was obtained. Full article
(This article belongs to the Special Issue Glycans in Virus-Host Interactions)
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12 pages, 8623 KiB  
Article
N-Glycan Profiles of Neuraminidase from Avian Influenza Viruses
by Wentian Chen, Tianran Ma, Sinuo Liu, Yaogang Zhong, Hanjie Yu, Jian Shu, Xiurong Wang and Zheng Li
Viruses 2024, 16(2), 190; https://doi.org/10.3390/v16020190 - 26 Jan 2024
Cited by 1 | Viewed by 1746
Abstract
The cleavage of sialic acids by neuraminidase (NA) facilitates the spread of influenza A virus (IV) descendants. Understanding the enzymatic activity of NA aids research into the transmission of IVs. An effective method for purifying NA was developed using p-aminophenyloxamic acid-modified functionalized [...] Read more.
The cleavage of sialic acids by neuraminidase (NA) facilitates the spread of influenza A virus (IV) descendants. Understanding the enzymatic activity of NA aids research into the transmission of IVs. An effective method for purifying NA was developed using p-aminophenyloxamic acid-modified functionalized hydroxylated magnetic particles (AAMPs), and from 0.299 to 0.401 mg of NA from eight IV strains was isolated by 1 mg AAMP. A combination of lectin microarrays and MALDI-TOF/TOF-MS was employed to investigate the N-glycans of isolated NAs. We found that more than 20 N-glycans were identified, and 16 glycan peaks were identical in the strains derived from chicken embryo cultivation. Multi-antennae, bisected, or core-fucosylated N-glycans are common in all the NAs. The terminal residues of N-glycans are predominantly composed of galactose and N-acetylglucosamine residues. Meanwhile, sialic acid residue was uncommon in these N-glycans. Further computational docking analysis predicted the interaction mechanism between NA and p-aminophenyloxamic acid. Full article
(This article belongs to the Special Issue Glycans in Virus-Host Interactions)
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Review

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16 pages, 1723 KiB  
Review
Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism
by Caroline K. Page and Stephen Mark Tompkins
Viruses 2024, 16(9), 1356; https://doi.org/10.3390/v16091356 - 24 Aug 2024
Viewed by 2049
Abstract
Influenza A and influenza B viruses (FLUAV and FLUBV, respectively) cause significant respiratory disease, hospitalization, and mortality each year. Despite causing at least 25% of the annual disease burden, FLUBV is historically understudied. Unlike FLUAVs, which possess pandemic potential due to their many [...] Read more.
Influenza A and influenza B viruses (FLUAV and FLUBV, respectively) cause significant respiratory disease, hospitalization, and mortality each year. Despite causing at least 25% of the annual disease burden, FLUBV is historically understudied. Unlike FLUAVs, which possess pandemic potential due to their many subtypes and broad host range, FLUBVs are thought to be restricted to only humans and are limited to two lineages. The hemagglutinins (HA) of both influenza types bind glycans terminating in α2,6- or α2,3-sialic acids. For FLUAV, the tropism of human- and avian-origin viruses is well-defined and determined by the terminal sialic acid configuration the HA can accommodate, with avian-origin viruses binding α2,3-linked sialic acids and human-origin viruses binding α2,6-linked sialic acids. In contrast, less is known about FLUBV receptor binding and its impact on host tropism. This review discusses the current literature on FLUBV receptor specificity, HA glycosylation, and their roles in virus tropism, evolution, and infection. While the focus is on findings in the past dozen years, it should be noted that the most current approaches for measuring virus–glycan interactions have not yet been applied to FLUBV and knowledge gaps remain. Full article
(This article belongs to the Special Issue Glycans in Virus-Host Interactions)
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23 pages, 1257 KiB  
Review
Back to the Basics of SARS-CoV-2 Biochemistry: Microvascular Occlusive Glycan Bindings Govern Its Morbidities and Inform Therapeutic Responses
by David E. Scheim, Peter I. Parry, David J. Rabbolini, Colleen Aldous, Morimasa Yagisawa, Robert Clancy, Thomas J. Borody and Wendy E. Hoy
Viruses 2024, 16(4), 647; https://doi.org/10.3390/v16040647 - 22 Apr 2024
Cited by 6 | Viewed by 7659
Abstract
Consistent with the biochemistry of coronaviruses as well established over decades, SARS-CoV-2 makes its initial attachment to host cells through the binding of its spike protein (SP) to sialylated glycans (containing the monosaccharide sialic acid) on the cell surface. The virus can then [...] Read more.
Consistent with the biochemistry of coronaviruses as well established over decades, SARS-CoV-2 makes its initial attachment to host cells through the binding of its spike protein (SP) to sialylated glycans (containing the monosaccharide sialic acid) on the cell surface. The virus can then slide over and enter via ACE2. SARS-CoV-2 SP attaches particularly tightly to the trillions of red blood cells (RBCs), platelets and endothelial cells in the human body, each cell very densely coated with sialic acid surface molecules but having no ACE2 or minimal ACE2. These interlaced attachments trigger the blood cell aggregation, microvascular occlusion and vascular damage that underlie the hypoxia, blood clotting and related morbidities of severe COVID-19. Notably, the two human betacoronaviruses that express a sialic acid-cleaving enzyme are benign, while the other three—SARS, SARS-CoV-2 and MERS—are virulent. RBC aggregation experimentally induced in several animal species using an injected polysaccharide caused most of the same morbidities of severe COVID-19. This glycan biochemistry is key to disentangling controversies that have arisen over the efficacy of certain generic COVID-19 treatment agents and the safety of SP-based COVID-19 vaccines. More broadly, disregard for the active physiological role of RBCs yields unreliable or erroneous reporting of pharmacokinetic parameters as routinely obtained for most drugs and other bioactive agents using detection in plasma, with whole-blood levels being up to 30-fold higher. Appreciation of the active role of RBCs can elucidate the microvascular underpinnings of other health conditions, including cardiovascular disease, and therapeutic opportunities to address them. Full article
(This article belongs to the Special Issue Glycans in Virus-Host Interactions)
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