Serveur d'exploration SRAS

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

Identifieur interne : 000B15 ( Ncbi/Merge ); précédent : 000B14; suivant : 000B16

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

Auteurs : Andrea Marzi [Allemagne] ; Thomas Gramberg ; Graham Simmons ; Peggy Möller ; Andrew J. Rennekamp ; Mandy Krumbiegel ; Martina Geier ; Jutta Eisemann ; Nadine Turza ; Bertrand Saunier ; Alexander Steinkasserer ; Stephan Becker ; Paul Bates ; Heike Hofmann ; Stefan Pöhlmann

Source :

RBID : pubmed:15479853

Descripteurs français

English descriptors

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.

DOI: 10.1128/JVI.78.21.12090-12095.2004
PubMed: 15479853

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pubmed:15479853

Le document en format XML

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<div type="abstract" xml:lang="en">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.</div>
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