Abstract：
: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.
journal_name
Naturejournal_title
Natureauthors
Ekiert DC,Kashyap AK,Steel J,Rubrum A,Bhabha G,Khayat R,Lee JH,Dillon MA,O'Neil RE,Faynboym AM,Horowitz M,Horowitz L,Ward AB,Palese P,Webby R,Lerner RA,Bhatt RR,Wilson IAdoi
10.1038/nature11414subject
Has Abstractpub_date
2012-09-27 00:00:00pages
526-32issue
7417eissn
0028-0836issn
1476-4687pii
nature11414journal_volume
489pub_type
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