Journal
VIROLOGY
Volume 448, Issue -, Pages 176-184Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2013.10.006
Keywords
Rhinovirus; Capsid structure; Model; I-Tasser; Rhinovirus C; Immunogenicity; Receptor binding
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Funding
- NIH [AI17331, U19 AI104317]
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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, ROBETFA, 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 Nimlab has increased the apparent selective pressure among the RV-C to fix mutations elsewhere in the VP1, creating a possible compensatory epitope. (C) 2013 Elsevier Inc. All rights reserved.
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