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J Virol. 2015 Jun;89(11):6136-40. doi: 10.1128/JVI.00433-15. Epub 2015 Mar 25.

Structure of Serotype 1 Reovirus Attachment Protein σ1 in Complex with Junctional Adhesion Molecule A Reveals a Conserved Serotype-Independent Binding Epitope.

Author information

1
Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
2
Department of Pathology, Microbiology, and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee, USA Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University School of Medicine, Nashville, Tennessee, USA Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee, USA thilo.stehle@uni-tuebingen.de terry.dermody@vanderbilt.edu.
3
Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, Tennessee, USA thilo.stehle@uni-tuebingen.de terry.dermody@vanderbilt.edu.

Abstract

Mammalian orthoreoviruses use glycans and junctional adhesion molecule A (JAM-A) as attachment receptors. We determined the structure of serotype 1 reovirus attachment protein σ1 alone and in complex with JAM-A. Comparison with the structure of serotype 3 reovirus σ1 bound to JAM-A reveals that both σ1 proteins engage JAM-A with similar affinities and via conserved binding epitopes. Thus, σ1-JAM-A interactions are unlikely to explain the differences in pathogenesis displayed by these reovirus serotypes.

PMID:
25810543
PMCID:
PMC4442426
DOI:
10.1128/JVI.00433-15
[Indexed for MEDLINE]
Free PMC Article

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