期刊
NATURE
卷 489, 期 7417, 页码 526-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature11414
关键词
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资金
- National Institutes of Health (NIH) [P01AI058113]
- Achievement Rewards for College Scientists Foundation [GM080209]
- NIH Molecular Evolution Training Program
- Skaggs Institute
- Northeast Biodefense Center [U54-AI057158-Lipkin]
- National Institute of Allergy and Infectious Diseases (NIAID) [U01AI070373]
- Center for Research on Influenza Pathogenesis NIAID [HHSN266200700010C]
- DOE Office of Biological and Environmental Research
- NIH, National Center for Research Resources, Biomedical Technology Program
- National Institute of General Medical Sciences (NIGMS)
- National Cancer Institute [Y1-CO-1020]
- NIGMS [Y1-GM-1104]
- US Department of Energy, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
- NIH though the P41 program at the National Center for Research Resources [RR017573]
- NIH [U54 GM094586]
Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the size and shape of protein surfaces that can be targeted. Single protein loops can mediate extremely high-affinity binding, but it is unclear whether such a mechanism is available to antibodies. Here we report the isolation and characterization of an antibody called C05, which neutralizes strains from multiple subtypes of influenza A virus, including H1, H2 and H3. X-ray and electron microscopy structures show that C05 recognizes conserved elements of the receptor-binding site on the haemagglutinin surface glycoprotein. Recognition of the haemagglutinin receptor-binding site is dominated by a single heavy-chain complementarity-determining region 3 loop, with minor contacts from heavy-chain complementarity-determining region 1, and is sufficient to achieve nanomolar binding with a minimal footprint. Thus, binding predominantly with a single loop can allow antibodies to target small, conserved functional sites on otherwise hypervariable antigens.
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