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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.
  • Lee CD; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
  • Watanabe Y; School of Biological Sciences, University of Southampton, Southampton, England, United Kingdom.
  • Wu NC; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, England, United Kingdom.
  • Han J; Division of Structural Biology, University of Oxford, Wellcome Centre for Human Genetics, Oxford, England, United Kingdom.
  • Kumar S; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
  • Pholcharee T; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
  • Seabright GE; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
  • Allen JD; Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, United States of America.
  • Lin CW; School of Biological Sciences, University of Southampton, Southampton, England, United Kingdom.
  • Yang JR; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, England, United Kingdom.
  • Liu MT; School of Biological Sciences, University of Southampton, Southampton, England, United Kingdom.
  • Wu CY; Department of Chemistry, The Scripps Research Institute, La Jolla, California, United States of America.
  • Ward AB; Centers for Disease Control, Taipei City, Taiwan.
  • Crispin M; Centers for Disease Control, Taipei City, Taiwan.
  • Wilson IA; Genomics Research Center, Academia Sinica, Taipei City, Taiwan.
PLoS Pathog ; 17(3): e1009407, 2021 03.
Article in English | MEDLINE | ID: covidwho-1338134
Semantic information from SemMedBD (by NLM)
1. Orthomyxoviridae PROCESS_OF human group
Subject
Orthomyxoviridae
Predicate
PROCESS_OF
Object
human group
2. Orthomyxoviridae LOCATION_OF Surface Antigens
Subject
Orthomyxoviridae
Predicate
LOCATION_OF
Object
Surface Antigens
3. Glycan Antibody INTERACTS_WITH HIV envelope protein
Subject
Glycan Antibody
Predicate
INTERACTS_WITH
Object
HIV envelope protein
4. Orthomyxoviridae INTERACTS_WITH Human virus
Subject
Orthomyxoviridae
Predicate
INTERACTS_WITH
Object
Human virus
5. Orthomyxoviridae PROCESS_OF human group
Subject
Orthomyxoviridae
Predicate
PROCESS_OF
Object
human group
6. Orthomyxoviridae LOCATION_OF Surface Antigens
Subject
Orthomyxoviridae
Predicate
LOCATION_OF
Object
Surface Antigens
7. Glycan Antibody INTERACTS_WITH HIV envelope protein
Subject
Glycan Antibody
Predicate
INTERACTS_WITH
Object
HIV envelope protein
8. Orthomyxoviridae INTERACTS_WITH Human virus
Subject
Orthomyxoviridae
Predicate
INTERACTS_WITH
Object
Human virus
ABSTRACT
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.
Subject(s)

Full text: Available Collection: International databases Database: MEDLINE Main subject: HIV-1 / Hemagglutinin Glycoproteins, Influenza Virus / Influenza A Virus, H3N2 Subtype / Antibodies, Viral Type of study: Randomized controlled trials Limits: Humans Language: English Journal: PLoS Pathog Year: 2021 Document Type: Article Affiliation country: Journal.ppat.1009407

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Full text: Available Collection: International databases Database: MEDLINE Main subject: HIV-1 / Hemagglutinin Glycoproteins, Influenza Virus / Influenza A Virus, H3N2 Subtype / Antibodies, Viral Type of study: Randomized controlled trials Limits: Humans Language: English Journal: PLoS Pathog Year: 2021 Document Type: Article Affiliation country: Journal.ppat.1009407