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.
Original language | English |
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Pages (from-to) | 224-236 |
Number of pages | 13 |
Journal | Virology |
Volume | 340 |
Issue number | 2 |
DOIs | |
Publication status | Published - 30 Sept 2005 |
Keywords
- receptor
- human immunodeficiency virus
- attachment factor
- DC-SIGN
- LSECtin
- hepatitis C virus
- glycoprotein
- ebolavirus
- SARS coronavirus
- DC-SIGNR