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. 1993 Aug 1;90(15):7015–7018. doi: 10.1073/pnas.90.15.7015

Structure of a human rhinovirus-bivalently bound antibody complex: implications for viral neutralization and antibody flexibility.

T J Smith 1, N H Olson 1, R H Cheng 1, E S Chase 1, T S Baker 1
PMCID: PMC47066  PMID: 8394005

Abstract

The structure of a neutralizing immunoglobulin (monoclonal antibody mAb17-IA), bound to human rhinovirus 14 (HRV14), has been determined by cryo-electron microscopy and image reconstruction. The antibody bound bivalently across icosahedral twofold axes of the virus, and there were no detectable conformational changes in the capsid. Thus, bivalently bound IgGs do not appear to cause gross deformations in the capsid. Differences between the electron density of the constant domains of the bound Fab fragment and IgG structures suggested that conformational changes occur about elbow axes upon bivalent attachment as was previously predicted. No significant density was observed for the Fc fragment, which adds further evidence for a high degree of mobility about the hinge region.

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