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LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus.

Identifieur interne : 004774 ( Main/Exploration ); précédent : 004773; suivant : 004775

LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus.

Auteurs : Thomas Gramberg [Allemagne] ; Heike Hofmann ; Peggy Möller ; Patricia F. Lalor ; Andrea Marzi ; Martina Geier ; Mandy Krumbiegel ; Thomas Winkler ; Frank Kirchhoff ; David H. Adams ; Stephan Becker ; Jan Münch ; Stefan Pöhlmann

Source :

RBID : pubmed:16051304

Descripteurs français

English descriptors

Abstract

Cellular attachment factors like the C-type lectins DC-SIGN and DC-SIGNR (collectively referred to as DC-SIGN/R) can augment viral infection and might promote viral dissemination in and between hosts. The lectin LSECtin is encoded in the same chromosomal locus as DC-SIGN/R and is coexpressed with DC-SIGNR on sinusoidal endothelial cells in liver and lymphnodes. Here, we show that LSECtin enhances infection driven by filovirus glycoproteins (GP) and the S protein of SARS coronavirus, but does not interact with human immunodeficiency virus type-1 and hepatitis C virus envelope proteins. Ligand binding to LSECtin was inhibited by EGTA but not by mannan, suggesting that LSECtin unlike DC-SIGN/R does not recognize high-mannose glycans on viral GPs. Finally, we demonstrate that LSECtin is N-linked glycosylated and that glycosylation is required for cell surface expression. In summary, we identified LSECtin as an attachment factor that in conjunction with DC-SIGNR might concentrate viral pathogens in liver and lymph nodes.

DOI: 10.1016/j.virol.2005.06.026
PubMed: 16051304


Affiliations:


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Le document en format XML

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<term>Filoviridae (metabolism)</term>
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<div type="abstract" xml:lang="en">Cellular attachment factors like the C-type lectins DC-SIGN and DC-SIGNR (collectively referred to as DC-SIGN/R) can augment viral infection and might promote viral dissemination in and between hosts. The lectin LSECtin is encoded in the same chromosomal locus as DC-SIGN/R and is coexpressed with DC-SIGNR on sinusoidal endothelial cells in liver and lymphnodes. Here, we show that LSECtin enhances infection driven by filovirus glycoproteins (GP) and the S protein of SARS coronavirus, but does not interact with human immunodeficiency virus type-1 and hepatitis C virus envelope proteins. Ligand binding to LSECtin was inhibited by EGTA but not by mannan, suggesting that LSECtin unlike DC-SIGN/R does not recognize high-mannose glycans on viral GPs. Finally, we demonstrate that LSECtin is N-linked glycosylated and that glycosylation is required for cell surface expression. In summary, we identified LSECtin as an attachment factor that in conjunction with DC-SIGNR might concentrate viral pathogens in liver and lymph nodes.</div>
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