1rvf: Difference between revisions
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==Overview== | ==Overview== | ||
The three-dimensional structure of intact human rhinovirus 14 (HRV-14) | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Poliovirus and Rhinovirus]] | [[Category: Poliovirus and Rhinovirus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Smith, T | [[Category: Smith, T J.]] | ||
[[Category: coat protein]] | [[Category: coat protein]] | ||
[[Category: complex (coat protein/immunoglobulin)]] | [[Category: complex (coat protein/immunoglobulin)]] | ||
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[[Category: thiol protease]] | [[Category: thiol protease]] | ||
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Revision as of 15:55, 21 February 2008
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FAB COMPLEXED WITH INTACT HUMAN RHINOVIRUS
OverviewOverview
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.
About this StructureAbout this Structure
1RVF is a Protein complex structure of sequences from Human rhinovirus 10, Human rhinovirus sp. and Mus musculus. The following page contains interesting information on the relation of 1RVF with [Poliovirus and Rhinovirus]. Full crystallographic information is available from OCA.
ReferenceReference
Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon., Smith TJ, Chase ES, Schmidt TJ, Olson NH, Baker TS, Nature. 1996 Sep 26;383(6598):350-4. PMID:8848050
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