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Antibody Recognition of a Highly Conserved Influenza Virus Epitope
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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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“The HA stem region is an attractive therapeutic epitope as it is highly conserved across all influenza A subtypes, and targeting this region can block the low-pH-induced conformational rearrangements associated with membrane fusion, which is essential for virus infection32,33.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [33]
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Self-citation
Metadata
- 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.
- Venue
- Science
- Published
- 2009-04-10
- Volume
- 324
- Issue
- 5924
- Pages
- 246-251
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- 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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