Journal article

Determinants of the Specificity of Rotavirus Interactions with the alpha 2 beta 1 Integrin

Fiona E Fleming, Kate L Graham, Yoshikazu Takada, Barbara S Coulson

JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2011

Abstract

The human α2β1 integrin binds collagen and acts as a cellular receptor for rotaviruses and human echovirus 1. These ligands require the inserted (I) domain within the α2 subunit of α2β1 for binding. Previous studies have identified the binding sites for collagen and echovirus 1 in the α2 I domain. We used CHO cells expressing mutated α2β1 to identify amino acids involved in binding to human and animal rotaviruses. Residues where mutation affected rotavirus binding were located in several exposed loops and adjacent regions of the α2 I domain. Binding by all rotaviruses was eliminated by mutations in the activation-responsive αC-α6 and αF helices. This is a novel feature that distinguishes rot..

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Grants

Awarded by National Institutes of Health


Awarded by National Health and Medical Research Council of Australia (NHMRC)


Awarded by NATIONAL CANCER INSTITUTE


Funding Acknowledgements

This work was supported, in whole or in part, by National Institutes of Health Grant 1R01CA131015-01A2 (to Y. T.) and Grants 350252, 350253, 509006, and 628319 (to B. S. C.) from the National Health and Medical Research Council of Australia (NHMRC).