Hepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNR

被引:302
作者
Pöhlmann, S
Zhang, J
Baribaud, F
Chen, ZW
Leslie, G
Lin, G
Granelli-Piperno, A
Dom, RW
Rice, CM
McsKeating, JA
机构
[1] Rockefeller Univ, Ctr Study Hepatitis C, Lab Virol & Infect Dis, New York, NY 10021 USA
[2] Rockefeller Univ, Cellular Physiol & Immunol Lab, New York, NY 10021 USA
[3] Univ Penn, Dept Microbiol, Div Hematol Oncol, Philadelphia, PA 19104 USA
[4] Univ Penn, Dept Med, Div Hematol Oncol, Philadelphia, PA 19104 USA
[5] Aaron Diamond AIDS Res Ctr, New York, NY 10016 USA
关键词
D O I
10.1128/JVI.77.7.4070-4080.2003
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
DC-SIGN and DC-SIGNR are two closely related membrane-associated C-type lectins that bind human immunodeficiency virus (HIV) envelope glycoprotein with high affinity. Binding of HIV to cells expressing DC-SIGN or DC-SIGNR can enhance the efficiency of infection of cells coexpressing the specific HIV receptors. DC-SIGN is expressed on some dendritic cells, while DC-SIGNR is localized to certain endothelial cell populations, including hepatic sinusoidal endothelial cells. We found that soluble versions of the hepatitis C virus (HCV) E2 glycoprotein and retrovirus pseudotypes expressing chimeric forms of both HCV El and E2 glycoproteins bound efficiently to DC-SIGN and DC-SIGNR expressed on cell lines and primary human endothelial cells but not to other C-type lectins tested. Soluble E2 bound to immature and mature human monocyte-derived dendritic cells (MDDCs). Binding of E2 to immature MDDCs was dependent on DC-SIGN interactions, while binding to mature MDDCs was partly independent of DC-SIGN, suggesting that other cell surface molecules may mediate HCV glycoprotein interactions. HCV interactions with DC-SIGN and DC-SIGNR may contribute to the establishment or persistence of infection both by the capture and delivery of virus to the liver and by modulating dendritic cell function.
引用
收藏
页码:4070 / 4080
页数:11
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