DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus

J Virol. 2004 Nov;78(21):12090-5. doi: 10.1128/JVI.78.21.12090-12095.2004.

Abstract

The lectins DC-SIGN and DC-SIGNR can augment viral infection; however, the range of pathogens interacting with these attachment factors is incompletely defined. Here we show that DC-SIGN and DC-SIGNR enhance infection mediated by the glycoprotein (GP) of Marburg virus (MARV) and the S protein of severe acute respiratory syndrome coronavirus and might promote viral dissemination. SIGNR1, a murine DC-SIGN homologue, also enhanced infection driven by MARV and Ebola virus GP and could be targeted to assess the role of attachment factors in filovirus infection in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Adhesion Molecules / physiology*
  • Glycoproteins / physiology*
  • Lectins, C-Type / physiology*
  • Marburgvirus / physiology*
  • Membrane Glycoproteins / physiology*
  • Receptors, Cell Surface / physiology*
  • SARS Virus / physiology*
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins / physiology*

Substances

  • CLEC4M protein, human
  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • Glycoproteins
  • Lectins, C-Type
  • Membrane Glycoproteins
  • Receptors, Cell Surface
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins
  • spike glycoprotein, SARS-CoV
  • spike protein, mouse hepatitis virus