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Structural evidence for common functions and ancestry of the reovirus and adenovirus attachment proteins
Author(s) -
Stehle Thilo,
Dermody Terence S.
Publication year - 2003
Publication title -
reviews in medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.06
H-Index - 90
eISSN - 1099-1654
pISSN - 1052-9276
DOI - 10.1002/rmv.379
Subject(s) - capsid , biology , virology , coxsackievirus , receptor , adenoviridae , protein structure , virus , flexibility (engineering) , microbiology and biotechnology , biophysics , genetics , enterovirus , recombinant dna , gene , biochemistry , statistics , mathematics
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.