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

A Marzi, T Gramberg, G Simmons, P Möller… - Journal of …, 2004 - journals.asm.org
A Marzi, T Gramberg, G Simmons, P Möller, AJ Rennekamp, M Krumbiegel, M Geier…
Journal of virology, 2004journals.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 …
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.
American Society for Microbiology