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

T Gramberg, H Hofmann, P Moller, Patricia Lalor, A Marzi, M Geier, M Krumbiegel, T Winkler, F Kirchhoff, David Adams, S Becker, J Much, S Pohlmann

Research output: Contribution to journalArticle

141 Citations (Scopus)


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 languageEnglish
Pages (from-to)224-236
Number of pages13
Issue number2
Publication statusPublished - 30 Sept 2005


  • receptor
  • human immunodeficiency virus
  • attachment factor
  • LSECtin
  • hepatitis C virus
  • glycoprotein
  • ebolavirus
  • SARS coronavirus


Dive into the research topics of 'LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus'. Together they form a unique fingerprint.

Cite this