Binding of Herpes Simplex Virus Glycoprotein B (gB) to Paired Immunoglobulin-Like Type 2 Receptor α Depends on Specific Sialylated O-Linked Glycans on gB

被引：53
作者：
Wang, Jing [1 ,2 ]
Fan, Qing [3 ]
Satoh, Takeshi [1 ,2 ]
Arii, Jun [4 ]
Lanier, Lewis L. [5 ,6 ]
Spear, Patricia G. [3 ]
Kawaguchi, Yasushi [4 ]
Arase, Hisashi [1 ,2 ]
机构：
[1] Osaka Univ, Lab Immunochem, WPI Immunol Frontier Res Ctr, Suita, Osaka 5650871, Japan
[2] Osaka Univ, Dept Immunochem, Microbial Dis Res Inst, Suita, Osaka 5650871, Japan
[3] Northwestern Univ, Dept Microbiol Immunol, Feinberg Sch Med, Chicago, IL 60611 USA
[4] Univ Tokyo, Dept Infect Dis Control, Int Res Ctr Infect Dis, Inst Med Sci,Minato Ku, Tokyo 1088639, Japan
[5] Univ Calif San Francisco, Dept Microbiol & Immunol, San Francisco, CA 94143 USA
[6] Univ Calif San Francisco, Canc Res Inst, San Francisco, CA 94143 USA
来源：
JOURNAL OF VIROLOGY | 2009年 / 83卷 / 24期
关键词：
GLYCOSYLATION; RECOGNITION; CELLS; CD99; PILR;
D O I：
10.1128/JVI.00792-09
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Paired immunoglobulin-like type 2 receptor alpha (PILR alpha) is an inhibitory receptor expressed on both hematopoietic and nonhematopoietic cells. Its binding to a cellular ligand, CD99, depends on the presence of sialylated O-linked glycans on CD99. Glycoprotein B (gB) of herpes simplex virus type 1 (HSV-1) binds to PILR alpha, and this association is involved in HSV-1 infection. Here, we found that the presence of sialylated O-glycans on gB is required for gB to associate with PILR alpha. Furthermore, we identified two threonine residues on gB that are essential for the addition of the principal O-glycans acquired by gB and that are also essential for the binding of PILR alpha to gB.
引用
收藏
页码：13042 / 13045
页数：4
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