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

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• 作者：Thomas Gramberg ; Heike Hofmann ; Peggy Mö ; ller ; Patricia F. Lalor ; Andrea Marzi ; Martina Geier ; Mandy Krumbiegel ; Thomas Winkler ; Frank Kirchhoff ; David H. Adams et al.
• 关键词：Ebolavirus ; SARS coronavirus ; Human immunodeficiency virus ; Hepatitis C virus ; LSECtin ; DC-SIGN ; DC-SIGNR ; Attachment factor ; Receptor ; Glycoprotein
• 刊名：Virology
• 出版年：2005
• 出版时间：2005
• 年：2005
• 卷：340
• 期：2
• 页码：224-236
• 全文大小：582 K

文摘

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.