Cited by 1,326Influenza Virus Research Studiesvaccines and immunoinformatics approachesMonoclonal and Polyclonal Antibodies Research

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Antibody Recognition of a Highly Conserved Influenza Virus Epitope

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Ekiert, Damian C., Bhabha, Gira, Elsliger, Marc-André, Friesen, Robert H. E., Jongeneelen, Mandy, Throsby, Mark, Goudsmit, Jaap, Wilson, Ian A.·2009·Science

DOI 10.1126/science.1171491PMC PMC2758658

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Abstract

Influenza virus presents an important and persistent threat to public health worldwide, and current vaccines provide immunity to viral isolates similar to the vaccine strain. High-affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Cocrystal structures were determined at 2.2 and 2.7 angstrom resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1 and HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.

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Authors: Ekiert, D. C., Bhabha, G., Elsliger, M.-A., Friesen, R. H. E., Jongeneelen, M., Throsby, M., Goudsmit, J., & Wilson, I. A.
Affiliations: Scripps Research Institute (US)
Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Corresponding author: Wilson, Ian A.
ORCID: Ekiert, Damian C.
Bhabha, Gira
Jongeneelen, Mandy
Throsby, Mark
Wilson, Ian A.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2009-04-10
Volume: 324
Issue: 5924
Pages: 246-251
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1171491
PMC: PMC2758658
OpenAlex: W2152617913
Cited by: 1,326
References: 39
Citations by year: 2026: 42 · 2025: 51 · 2024: 40 · 2023: 50 · 2022: 57 · 2021: 73 · 2020: 86 · 2019: 66 · 2018: 75 · 2017: 72 · 2016: 81 · 2015: 90 · 2014: 93 · 2013: 133 · 2012: 110
FWCI: 70.96
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Science (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Pure Amsterdam UMC (submittedVersion)
Funders: National Cancer Institute (Y1-CO-1020)
National Institute of General Medical Sciences (Y1-GM-1104, U54GM074898)
National Institute of Allergy and Infectious Diseases (P01AI058113, AI058113)
Topics: Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Keywords: influenza virus, broadly neutralizing antibodies, hemagglutinin, conserved epitopes, H5N1 avian influenza, antibody-antigen complex structure, vaccine design, antibody-based therapy
MeSH terms: Antibodies, Viral, Antibody Affinity, Epitopes, Antigens, Viral, Binding Sites, Antibody, Crystallization, Glycosylation, Humans, Hydrogen Bonding, Hydrogen-Ion Concentration, Immunoglobulin Fab Fragments, Influenza Vaccines, Membrane Fusion, Models, Molecular, Neutralization Tests, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Hemagglutinin Glycoproteins, Influenza Virus, Influenza A Virus, H1N1 Subtype, Influenza A Virus, H5N1 Subtype, Hydrophobic and Hydrophilic Interactions

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