DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus.
Identifieur interne : 005396 ( Main/Exploration ); précédent : 005395; suivant : 005397DC-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 PöhlmannSource :
- Journal of virology [ 0022-538X ] ; 2004.
Descripteurs français
- KwdFr :
- Glycoprotéine de spicule des coronavirus, Glycoprotéines (physiologie), Glycoprotéines membranaires (physiologie), Lectines de type C (physiologie), Marburgvirus (physiologie), Molécules d'adhérence cellulaire (physiologie), Protéines de l'enveloppe virale (physiologie), Récepteurs de surface cellulaire (physiologie), Virus du SRAS (physiologie).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , physiology : Cell Adhesion Molecules, Glycoproteins, Lectins, C-Type, Membrane Glycoproteins, Receptors, Cell Surface, Viral Envelope Proteins.
- physiology : Marburgvirus, SARS Virus.
- chemical : Spike Glycoprotein, Coronavirus.
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
Affiliations:
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Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en">DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus.</title>
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<term>Marburgvirus (physiology)</term>
<term>Membrane Glycoproteins (physiology)</term>
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<term>Membrane Glycoproteins</term>
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<front><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>
</front>
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<country name="Allemagne"><noRegion><name sortKey="Marzi, Andrea" sort="Marzi, Andrea" uniqKey="Marzi A" first="Andrea" last="Marzi">Andrea Marzi</name>
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