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Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5057, CEA-CNRS-UJF, 41 rue Jules Horowitz, 38027 Grenoble, France,1 Max F. Perutz Laboratories, Vienna Biocenter, Medical University of Vienna, Dr Bohr Gasse 9/3, A-1030 Vienna, Austria2
Received 4 July 2006/ Accepted 15 September 2006
The monoclonal antibody 2G2 has been used extensively for detection and quantification of structural changes of human rhinovirus serotype 2 during infection. It recognizes exclusively A and B subviral particles, not native virus. We have elucidated the basis of this selectivity by determining the footprint of 2G2. Since viral escape mutants obviously cannot be obtained, the structures of complexes between Fab fragments of 2G2 and 80S subviral B particles were determined by cryoelectron microscopy. The footprint of the antibody corresponds to the capsid region that we predicted would undergo the most dramatic changes upon RNA release.
Published ahead of print on 27 September 2006.
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
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| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
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