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. 2003 Feb 28;13(2):123–132. doi: 10.1002/rmv.379

Structural evidence for common functions and ancestry of the reovirus and adenovirus attachment proteins

Thilo Stehle 1,✉, Terence S Dermody 2,✉
PMCID: PMC7169122  PMID: 12627395

Abstract

The crystal structure of the reovirus attachment protein, σ1, reveals a fibre‐like structure that is remarkably similar to that of the adenovirus attachment protein, fibre. Both proteins are trimers with head‐and‐tail morphology. They share unique domain structures and functional properties including defined regions of flexibility within the tail and an unusual symmetry mismatch with the pentameric viral capsid protein into which they are inserted. Moreover, the receptors for reoviruses and adenoviruses, junctional adhesion molecule 1 and coxsackievirus and adenovirus receptor, respectively, also share key structural and functional properties. Although reoviruses and adenoviruses belong to different virus families and have few properties in common, the observed similarities between σ1 and fibre point to a conserved mechanism of attachment and an ancient evolutionary relationship. Copyright © 2003 John Wiley & Sons, Ltd.

Contributor Information

Thilo Stehle, Email: tstehle@partners.org.

Terence S. Dermody, Email: terry.dermody@vanderbilt.edu.

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