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

Stehle T, Dermody TS
Rev Med Virol. 2003 13 (2): 123-32

PMID: 12627395 · PMCID: PMC7169122 · DOI:10.1002/rmv.379

The crystal structure of the reovirus attachment protein, sigma1, 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 sigma1 and fibre point to a conserved mechanism of attachment and an ancient evolutionary relationship.

Copyright 2003 John Wiley & Sons, Ltd.

MeSH Terms (13)

Adenoviridae Animals Capsid Proteins Cell Adhesion Molecules Coxsackie and Adenovirus Receptor-Like Membrane Protein Evolution, Molecular Humans Junctional Adhesion Molecules Mice Models, Molecular Receptors, Virus Reoviridae Viral Nonstructural Proteins

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