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

  • Stettner E
  • Dietrich M
  • Reiss K
  • et al.
21Citations
Citations of this article
18Readers
Mendeley users who have this article in their library.

This article is free to access.

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.

Cite

CITATION STYLE

APA

Stettner, E., Dietrich, M. H., Reiss, K., Dermody, T. S., & Stehle, T. (2015). Structure of Serotype 1 Reovirus Attachment Protein σ1 in Complex with Junctional Adhesion Molecule A Reveals a Conserved Serotype-Independent Binding Epitope. Journal of Virology, 89(11), 6136–6140. https://doi.org/10.1128/jvi.00433-15

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free