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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus. Gramberg, T., Hofmann, H., Möller, P., Lalor, P.F., Marzi, A., Geier, M., Krumbiegel, M., Winkler, T., Kirchhoff, F., Adams, D.H., Becker, S., Münch, J., Pöhlmann, S. Virology (2005) [Pubmed]
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