期刊
JOURNAL OF VIROLOGY
卷 80, 期 3, 页码 1290-1301出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.80.3.1290-1301.2006
关键词
-
类别
资金
- NCRR NIH HHS [F31 RR005074, F31 RR 05074] Funding Source: Medline
- NIAID NIH HHS [T32 AI007632, T32 AI 07632, U54 AI057168, AI 50469, T32 AI 07324-13, U54 AI 57168, T32 AI007324, R01 AI050469] Funding Source: Medline
- NIGMS NIH HHS [T32 GM007229, T32 GM 007229] Funding Source: Medline
The C-type lectins DC-SIGN and DC-SIGNR bind mannose-rich glycans with high affinity. In vitro, cells expressing these attachment factors efficiently capture, and are infected by, a diverse array of appropriately glycosylated pathogens, including dengue virus. In this study, we investigated whether these lectins could enhance cellular infection by West Nile virus (WNV), a mosquito-borne flavivirus related to dengue virus. We discovered that DC-SIGNR promoted WNV infection much more efficiently than did DC-SIGN, particularly when the virus was grown in human cell types. The presence of a single N-linked glycosylation site on either the prM or E glycoprotein of WNV was sufficient to allow DC-SIGNR-mediated infection, demonstrating that uncleaved prM protein present on a flavivirus virion can influence viral tropism under certain circumstances. Preferential utilization of DC-SIGNR was a specific property conferred by the WNV envelope glycoproteins. Chimeras between DC-SIGN and DC-SIGNR demonstrated that the ability of DC-SIGNR to promote WNV infection maps to its carbohydrate recognition domain. WNV virions and subviral particles bound to DC-SIGNR with much greater affinity than DC-SIGN. We believe this is the first report of a pathogen interacting more efficiently with DC-SIGNR than with DC-SIGN. Our results should lead to the discovery of new mechanisms by which these well-studied lectins discriminate among ligands.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据