LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus.
Identifieur interne : 004774 ( Main/Exploration ); précédent : 004773; suivant : 004775LSECtin 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 PöhlmannSource :
- Virology [ 0042-6822 ] ; 2005.
Descripteurs français
- KwdFr :
- Amorces ADN, Cadres ouverts de lecture, Cellules endothéliales (virologie), Filoviridae (génétique), Filoviridae (métabolisme), Foie (cytologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Lectines de type C (métabolisme), Lignée cellulaire, Mutagenèse, Protéines de l'enveloppe virale (métabolisme), Protéines virales (métabolisme), Rein, Réaction de polymérisation en chaîne, Séquence nucléotidique, Virus du SRAS (métabolisme).
- MESH :
- cytologie : Foie.
- génétique : Filoviridae.
- métabolisme : Filoviridae, Glycoprotéines membranaires, Lectines de type C, Protéines de l'enveloppe virale, Protéines virales, Virus du SRAS.
- virologie : Cellules endothéliales.
- Amorces ADN, Cadres ouverts de lecture, Glycoprotéine de spicule des coronavirus, Humains, Lignée cellulaire, Mutagenèse, Rein, Réaction de polymérisation en chaîne, Séquence nucléotidique.
English descriptors
- KwdEn :
- Base Sequence, Cell Line, DNA Primers, Endothelial Cells (virology), Filoviridae (genetics), Filoviridae (metabolism), Humans, Kidney, Lectins, C-Type (metabolism), Liver (cytology), Membrane Glycoproteins (metabolism), Mutagenesis, Open Reading Frames, Polymerase Chain Reaction, SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism), Viral Proteins (metabolism).
- MESH :
- chemical , metabolism : Lectins, C-Type, Membrane Glycoproteins, Viral Envelope Proteins, Viral Proteins.
- chemical : DNA Primers, Spike Glycoprotein, Coronavirus.
- cytology : Liver.
- genetics : Filoviridae.
- metabolism : Filoviridae, SARS Virus.
- virology : Endothelial Cells.
- Base Sequence, Cell Line, Humans, Kidney, Mutagenesis, Open Reading Frames, Polymerase Chain Reaction.
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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<front><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>
</front>
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<name sortKey="Geier, Martina" sort="Geier, Martina" uniqKey="Geier M" first="Martina" last="Geier">Martina Geier</name>
<name sortKey="Hofmann, Heike" sort="Hofmann, Heike" uniqKey="Hofmann H" first="Heike" last="Hofmann">Heike Hofmann</name>
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