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A cross-neutralizing antibody between HIV-1 and influenza virus
Incessant antigenic evolution enables the persistence and spread of influenza virus in the human population. As the principal target of the immune response, the hemagglutinin (HA) surface antigen on influenza viruses continuously acquires and replaces N-linked glycosylation sites to shield immunogen...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8016226/ https://www.ncbi.nlm.nih.gov/pubmed/33750987 http://dx.doi.org/10.1371/journal.ppat.1009407 |
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author | Lee, Chang-Chun D. Watanabe, Yasunori Wu, Nicholas C. Han, Julianna Kumar, Sonu Pholcharee, Tossapol Seabright, Gemma E. Allen, Joel D. Lin, Chih-Wei Yang, Ji-Rong Liu, Ming-Tsan Wu, Chung-Yi Ward, Andrew B. Crispin, Max Wilson, Ian A. |
author_facet | Lee, Chang-Chun D. Watanabe, Yasunori Wu, Nicholas C. Han, Julianna Kumar, Sonu Pholcharee, Tossapol Seabright, Gemma E. Allen, Joel D. Lin, Chih-Wei Yang, Ji-Rong Liu, Ming-Tsan Wu, Chung-Yi Ward, Andrew B. Crispin, Max Wilson, Ian A. |
author_sort | Lee, Chang-Chun D. |
collection | PubMed |
description | Incessant antigenic evolution enables the persistence and spread of influenza virus in the human population. As the principal target of the immune response, the hemagglutinin (HA) surface antigen on influenza viruses continuously acquires and replaces N-linked glycosylation sites to shield immunogenic protein epitopes using host-derived glycans. Anti-glycan antibodies, such as 2G12, target the HIV-1 envelope protein (Env), which is even more extensively glycosylated and contains under-processed oligomannose-type clusters on its dense glycan shield. Here, we illustrate that 2G12 can also neutralize human seasonal influenza A H3N2 viruses that have evolved to present similar oligomannose-type clusters on their HAs from around 20 years after the 1968 pandemic. Using structural biology and mass spectrometric approaches, we find that two N-glycosylation sites close to the receptor binding site (RBS) on influenza hemagglutinin represent the oligomannose cluster recognized by 2G12. One of these glycan sites is highly conserved in all human H3N2 strains and the other emerged during virus evolution. These two N-glycosylation sites have also become crucial for fitness of recent H3N2 strains. These findings shed light on the evolution of the glycan shield on influenza virus and suggest 2G12-like antibodies can potentially act as broad neutralizers to target human enveloped viruses. |
format | Online Article Text |
id | pubmed-8016226 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-80162262021-04-08 A cross-neutralizing antibody between HIV-1 and influenza virus Lee, Chang-Chun D. Watanabe, Yasunori Wu, Nicholas C. Han, Julianna Kumar, Sonu Pholcharee, Tossapol Seabright, Gemma E. Allen, Joel D. Lin, Chih-Wei Yang, Ji-Rong Liu, Ming-Tsan Wu, Chung-Yi Ward, Andrew B. Crispin, Max Wilson, Ian A. PLoS Pathog Research Article Incessant antigenic evolution enables the persistence and spread of influenza virus in the human population. As the principal target of the immune response, the hemagglutinin (HA) surface antigen on influenza viruses continuously acquires and replaces N-linked glycosylation sites to shield immunogenic protein epitopes using host-derived glycans. Anti-glycan antibodies, such as 2G12, target the HIV-1 envelope protein (Env), which is even more extensively glycosylated and contains under-processed oligomannose-type clusters on its dense glycan shield. Here, we illustrate that 2G12 can also neutralize human seasonal influenza A H3N2 viruses that have evolved to present similar oligomannose-type clusters on their HAs from around 20 years after the 1968 pandemic. Using structural biology and mass spectrometric approaches, we find that two N-glycosylation sites close to the receptor binding site (RBS) on influenza hemagglutinin represent the oligomannose cluster recognized by 2G12. One of these glycan sites is highly conserved in all human H3N2 strains and the other emerged during virus evolution. These two N-glycosylation sites have also become crucial for fitness of recent H3N2 strains. These findings shed light on the evolution of the glycan shield on influenza virus and suggest 2G12-like antibodies can potentially act as broad neutralizers to target human enveloped viruses. Public Library of Science 2021-03-22 /pmc/articles/PMC8016226/ /pubmed/33750987 http://dx.doi.org/10.1371/journal.ppat.1009407 Text en © 2021 Lee et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Lee, Chang-Chun D. Watanabe, Yasunori Wu, Nicholas C. Han, Julianna Kumar, Sonu Pholcharee, Tossapol Seabright, Gemma E. Allen, Joel D. Lin, Chih-Wei Yang, Ji-Rong Liu, Ming-Tsan Wu, Chung-Yi Ward, Andrew B. Crispin, Max Wilson, Ian A. A cross-neutralizing antibody between HIV-1 and influenza virus |
title | A cross-neutralizing antibody between HIV-1 and influenza virus |
title_full | A cross-neutralizing antibody between HIV-1 and influenza virus |
title_fullStr | A cross-neutralizing antibody between HIV-1 and influenza virus |
title_full_unstemmed | A cross-neutralizing antibody between HIV-1 and influenza virus |
title_short | A cross-neutralizing antibody between HIV-1 and influenza virus |
title_sort | cross-neutralizing antibody between hiv-1 and influenza virus |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8016226/ https://www.ncbi.nlm.nih.gov/pubmed/33750987 http://dx.doi.org/10.1371/journal.ppat.1009407 |
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