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

T. J. Smith, E. S. Chase, T. J. Schmidt, N. H. Olson, T. S. Baker

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Abstract

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 Å 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.

Original languageEnglish (US)
Pages (from-to)350-354
Number of pages5
JournalNature
Volume383
Issue number6598
DOIs
StatePublished - Oct 7 1996
Externally publishedYes

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Smith, T. J., Chase, E. S., Schmidt, T. J., Olson, N. H., & Baker, T. S. (1996). Neutralizing antibody to human rhinovirus 14 penetrates the receptor- binding canyon. Nature, 383(6598), 350-354. https://doi.org/10.1038/383350a0