Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon

Nature. 1996 Sep 26;383(6598):350-4. doi: 10.1038/383350a0.


The three-dimensional structure of intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fab17-IA) from a strongly neutralizing antibody that binds bivalently to the virion has been determined to 4.0 angstrom resolution by a combination of X-ray crystallography and cryo-electron microscopy. In contradiction to the most commonly held model of antibody-mediated neutralization, Fab17-IA does not induce a conformational change in the HRV-14 capsid. Instead, the paratope of the antibody undergoes a large conformational change to accommodate the epitope. Unlike any previously described antibody-antigen structure, the conserved framework region of the antibody makes extensive contact with the viral surface. Fab17-IA penetrates deep within the canyon in which the cellular receptor for HRV-14 binds. Hence, it is unlikely that viral quaternary structure evolves merely to evade immune recognition. Instead, the shape and position of the receptor-binding region on a virus probably dictates receptor binding and subsequent uncoating events and has little or no influence on concealing the virus from the immune system.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Monoclonal / chemistry
  • Antibodies, Monoclonal / immunology
  • Antibodies, Viral / chemistry*
  • Antibodies, Viral / immunology
  • Antigen-Antibody Complex / chemistry*
  • Binding Sites, Antibody
  • Capsid / chemistry
  • Capsid / immunology
  • Crystallography, X-Ray
  • Epitopes, B-Lymphocyte / chemistry
  • Humans
  • Immunoglobulin Fab Fragments / chemistry
  • Immunoglobulin Fab Fragments / immunology
  • Intercellular Adhesion Molecule-1 / chemistry
  • Models, Molecular
  • Neutralization Tests
  • Protein Conformation
  • Rhinovirus / chemistry*
  • Rhinovirus / immunology


  • Antibodies, Monoclonal
  • Antibodies, Viral
  • Antigen-Antibody Complex
  • Epitopes, B-Lymphocyte
  • Immunoglobulin Fab Fragments
  • Intercellular Adhesion Molecule-1