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Virology. 2014 Jan 5;448:176-84. doi: 10.1016/j.virol.2013.10.006. Epub 2013 Oct 25.

Modeling of the human rhinovirus C capsid suggests a novel topography with insights on receptor preference and immunogenicity.

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  • 1Institute for Molecular Virology, University of Wisconsin, Madison, USA.


Features of human rhinovirus (RV)-C virions that allow them to use novel cell receptors and evade immune responses are unknown. Unlike the RV-A+B, these isolates cannot be propagated in typical culture systems or grown for structure studies. Comparative sequencing, I-TASSER, MODELLER, ROBETTA, and refined alignment techniques led to a structural approximation for C15 virions, based on the extensive, resolved RV-A+B datasets. The model predicts that all RV-C VP1 proteins are shorter by 21 residues relative to the RV-A, and 35 residues relative to the RV-B, effectively shaving the RV 5-fold plateau from the particle. There are major alterations in VP1 neutralizing epitopes and the structural determinants for ICAM-1 and LDLR receptors. The VP2 and VP3 elements are similar among all RV, but the loss of sequence "words" contributing Nim1ab has increased the apparent selective pressure among the RV-C to fix mutations elsewhere in the VP1, creating a possible compensatory epitope.

© 2013 Elsevier Inc. All rights reserved.


Capsid structure; I-Tasser; Immunogenicity; Model; Receptor binding; Rhinovirus; Rhinovirus C

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