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Structure paper

TitleCross-neutralization of influenza A viruses mediated by a single antibody loop.
Journal, issue, pagesNature, Vol. 489, Issue 7417, Page 526-532, Year 2012
Publish dateSep 27, 2012
AuthorsDamian C Ekiert / Arun K Kashyap / John Steel / Adam Rubrum / Gira Bhabha / Reza Khayat / Jeong Hyun Lee / Michael A Dillon / Ryann E O'Neil / Aleksandr M Faynboym / Michael Horowitz / Lawrence Horowitz / Andrew B Ward / Peter Palese / Richard Webby / Richard A Lerner / Ramesh R Bhatt / Ian A Wilson /
PubMed AbstractImmune 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 ...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.
External linksNature / PubMed:22982990 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.901 - 17.0 Å
Structure data

EMDB-2138:
EM map of influenza H1 hemagglutatin in complex with C05 Fab
Method: EM (single particle) / Resolution: 17.0 Å

EMDB-2139:
EM map of an influenza H3 hemagglutatin in complex with C05 Fab
Method: EM (single particle) / Resolution: 17.0 Å

EMDB-2140:
EM map of influenza H2 hemagglutatin in complex with C05 Fab
Method: EM (single particle) / Resolution: 17.0 Å

PDB-4fnk:
Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin
Method: X-RAY DIFFRACTION / Resolution: 1.901 Å

PDB-4fnl:
Crystal structure of broadly neutralizing antibody C05
Method: X-RAY DIFFRACTION / Resolution: 2.297 Å

PDB-4fp8:
Crystal structure of broadly neutralizing antibody C05 bound to H3 influenza hemagglutinin, HA1 subunit
Method: X-RAY DIFFRACTION / Resolution: 2.947 Å

PDB-4fqr:
Crystal structure of broadly neutralizing antibody C05 bound to H3 influenza hemagglutinin
Method: X-RAY DIFFRACTION / Resolution: 4.1 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM / Tris

ChemComp-ZN:
Unknown entry

Source
  • Influenza A virus (A/Solomon Islands/3/2006(H1N1))
  • homo sapiens (human)
  • influenza a virus
  • Influenza A virus (A/Japan/305/1957(H2N2))
KeywordsVIRAL PROTEIN / viral fusion protein / virus attachment and entry / IMMUNE SYSTEM / Immunoglobulin / immune recognition / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex

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