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Conserved topology of virus glycoepitopes presents novel targets for repurposing HIV antibody 2G12
by
Raman, Rahul
, Subramanian, Vidya
, Sasisekharan, Ram
, Clark, Thomas
, Miller, Nathaniel L.
in
631/154
/ 631/535
/ Animals
/ Antibodies, Monoclonal - metabolism
/ Broadly Neutralizing Antibodies - metabolism
/ Dogs
/ Drug Repositioning
/ Epitopes
/ Glycoprotein gp120
/ Hemagglutinin Glycoproteins, Influenza Virus - metabolism
/ HIV
/ HIV Antibodies - metabolism
/ Human immunodeficiency virus
/ Humanities and Social Sciences
/ Humans
/ Influenza
/ Influenza A
/ Influenza A Virus, H1N1 Subtype - immunology
/ Influenza A Virus, H1N1 Subtype - metabolism
/ Influenza A Virus, H3N2 Subtype - immunology
/ Influenza A Virus, H3N2 Subtype - metabolism
/ Madin Darby Canine Kidney Cells
/ Mannose
/ Models, Immunological
/ Molecular Targeted Therapy
/ multidisciplinary
/ Neutralization Tests
/ Polysaccharides
/ Polysaccharides - metabolism
/ Protein structure
/ Proteins
/ SARS-CoV-2 - immunology
/ Science
/ Science (multidisciplinary)
/ Severe acute respiratory syndrome coronavirus 2
/ Therapeutic applications
/ Topology
/ Viruses
2022
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Conserved topology of virus glycoepitopes presents novel targets for repurposing HIV antibody 2G12
by
Raman, Rahul
, Subramanian, Vidya
, Sasisekharan, Ram
, Clark, Thomas
, Miller, Nathaniel L.
in
631/154
/ 631/535
/ Animals
/ Antibodies, Monoclonal - metabolism
/ Broadly Neutralizing Antibodies - metabolism
/ Dogs
/ Drug Repositioning
/ Epitopes
/ Glycoprotein gp120
/ Hemagglutinin Glycoproteins, Influenza Virus - metabolism
/ HIV
/ HIV Antibodies - metabolism
/ Human immunodeficiency virus
/ Humanities and Social Sciences
/ Humans
/ Influenza
/ Influenza A
/ Influenza A Virus, H1N1 Subtype - immunology
/ Influenza A Virus, H1N1 Subtype - metabolism
/ Influenza A Virus, H3N2 Subtype - immunology
/ Influenza A Virus, H3N2 Subtype - metabolism
/ Madin Darby Canine Kidney Cells
/ Mannose
/ Models, Immunological
/ Molecular Targeted Therapy
/ multidisciplinary
/ Neutralization Tests
/ Polysaccharides
/ Polysaccharides - metabolism
/ Protein structure
/ Proteins
/ SARS-CoV-2 - immunology
/ Science
/ Science (multidisciplinary)
/ Severe acute respiratory syndrome coronavirus 2
/ Therapeutic applications
/ Topology
/ Viruses
2022
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Conserved topology of virus glycoepitopes presents novel targets for repurposing HIV antibody 2G12
by
Raman, Rahul
, Subramanian, Vidya
, Sasisekharan, Ram
, Clark, Thomas
, Miller, Nathaniel L.
in
631/154
/ 631/535
/ Animals
/ Antibodies, Monoclonal - metabolism
/ Broadly Neutralizing Antibodies - metabolism
/ Dogs
/ Drug Repositioning
/ Epitopes
/ Glycoprotein gp120
/ Hemagglutinin Glycoproteins, Influenza Virus - metabolism
/ HIV
/ HIV Antibodies - metabolism
/ Human immunodeficiency virus
/ Humanities and Social Sciences
/ Humans
/ Influenza
/ Influenza A
/ Influenza A Virus, H1N1 Subtype - immunology
/ Influenza A Virus, H1N1 Subtype - metabolism
/ Influenza A Virus, H3N2 Subtype - immunology
/ Influenza A Virus, H3N2 Subtype - metabolism
/ Madin Darby Canine Kidney Cells
/ Mannose
/ Models, Immunological
/ Molecular Targeted Therapy
/ multidisciplinary
/ Neutralization Tests
/ Polysaccharides
/ Polysaccharides - metabolism
/ Protein structure
/ Proteins
/ SARS-CoV-2 - immunology
/ Science
/ Science (multidisciplinary)
/ Severe acute respiratory syndrome coronavirus 2
/ Therapeutic applications
/ Topology
/ Viruses
2022
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Conserved topology of virus glycoepitopes presents novel targets for repurposing HIV antibody 2G12
Journal Article
Conserved topology of virus glycoepitopes presents novel targets for repurposing HIV antibody 2G12
2022
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Overview
Complex glycans decorate viral surface proteins and play a critical role in virus–host interactions. Viral surface glycans shield vulnerable protein epitopes from host immunity yet can also present distinct “glycoepitopes” that can be targeted by host antibodies such as the potent anti-HIV antibody 2G12 that binds high-mannose glycans on gp120. Two recent publications demonstrate 2G12 binding to high mannose glycans on SARS-CoV-2 and select Influenza A (Flu) H3N2 viruses. Previously, our lab observed 2G12 binding and functional inhibition of a range of Flu viruses that include H3N2 and H1N1 lineages. In this manuscript, we present these data alongside structural analyses to offer an expanded picture of 2G12-Flu interactions. Further, based on the remarkable breadth of 2G12 N-glycan recognition and the structural factors promoting glycoprotein oligomannosylation, we hypothesize that 2G12 glycoepitopes can be defined from protein structure alone according to N-glycan
site
topology. We develop a model describing 2G12 glycoepitopes based on N-glycan site topology, and apply the model to identify viruses within the Protein Data Bank presenting putative 2G12 glycoepitopes for 2G12 repurposing toward analytical, diagnostic, and therapeutic applications.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/535
/ Animals
/ Antibodies, Monoclonal - metabolism
/ Broadly Neutralizing Antibodies - metabolism
/ Dogs
/ Epitopes
/ Hemagglutinin Glycoproteins, Influenza Virus - metabolism
/ HIV
/ Human immunodeficiency virus
/ Humanities and Social Sciences
/ Humans
/ Influenza A Virus, H1N1 Subtype - immunology
/ Influenza A Virus, H1N1 Subtype - metabolism
/ Influenza A Virus, H3N2 Subtype - immunology
/ Influenza A Virus, H3N2 Subtype - metabolism
/ Madin Darby Canine Kidney Cells
/ Mannose
/ Polysaccharides - metabolism
/ Proteins
/ Science
/ Severe acute respiratory syndrome coronavirus 2
/ Topology
/ Viruses
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