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

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

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Capsid Proteins / chemistry*
  • Crystallography, X-Ray
  • Junctional Adhesion Molecule A / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Receptors, Virus / chemistry*
  • Sequence Homology

Substances

  • Capsid Proteins
  • Junctional Adhesion Molecule A
  • Receptors, Virus
  • sigma 1 protein, reovirus

Associated data

  • PDB/1NBQ
  • PDB/3EOY
  • PDB/4GU3