DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus
Journal of virology, 2004•journals.asm.org
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 …
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 …
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.
