Author: Marzi, Andrea; Gramberg, Thomas; Simmons, Graham; Möller, Peggy; Rennekamp, Andrew J; Krumbiegel, Mandy; Geier, Martina; Eisemann, Jutta; Turza, Nadine; Saunier, Bertrand; Steinkasserer, Alexander; Becker, Stephan; Bates, Paul; Hofmann, Heike; Pöhlmann, Stefan
Title: DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus. Cord-id: astr06wk Document date: 2004_1_1
ID: astr06wk
Snippet: 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
Document: 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.
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