Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Adenoviridae / genetics
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Adenoviridae / physiology*
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Animals
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Capsid Proteins / chemistry*
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Capsid Proteins / genetics
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Capsid Proteins / metabolism
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Cell Adhesion Molecules / chemistry
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Cell Adhesion Molecules / genetics
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Cell Adhesion Molecules / metabolism
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Coxsackie and Adenovirus Receptor-Like Membrane Protein
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Evolution, Molecular*
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Humans
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Junctional Adhesion Molecules
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Mice
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Models, Molecular
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Receptors, Virus / chemistry
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Receptors, Virus / genetics
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Receptors, Virus / metabolism
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Reoviridae / genetics
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Reoviridae / physiology*
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Viral Nonstructural Proteins / chemistry*
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Viral Nonstructural Proteins / genetics
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Viral Nonstructural Proteins / metabolism
Substances
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CLMP protein, human
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CLMP protein, mouse
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Capsid Proteins
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Cell Adhesion Molecules
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Coxsackie and Adenovirus Receptor-Like Membrane Protein
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Junctional Adhesion Molecules
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Receptors, Virus
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Viral Nonstructural Proteins
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hexon capsid protein, Adenovirus
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sigma 1NS protein, Reovirus