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

Author:

Wang Jing12,Fan Qing3,Satoh Takeshi12,Arii Jun4,Lanier Lewis L.5,Spear Patricia G.3,Kawaguchi Yasushi4,Arase Hisashi12

Affiliation:

1. Department of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan

2. Laboratory of Immunochemistry, WPI Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, Japan

3. Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611

4. Department of Infectious Disease Control, International Research Center for Infectious Diseases, The Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan

5. Department of Microbiology and Immunology and the Cancer Research Institute, University of California, San Francisco, San Francisco, California 94143

Abstract

ABSTRACT Paired immunoglobulin-like type 2 receptor α (PILRα) 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 PILRα, 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 PILRα. 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 PILRα to gB.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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