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

Virology. 2005 Sep 30;340(2):224-36. doi: 10.1016/j.virol.2005.06.026.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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*


  • CLEC4G protein, human
  • DNA Primers
  • Lectins, C-Type
  • Membrane Glycoproteins
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins
  • Viral Proteins
  • spike glycoprotein, SARS-CoV
  • spike protein, mouse hepatitis virus