Binding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor alpha depends on specific sialylated O-linked glycans on gB.
Paired immunoglobulin-like type 2 receptor alpha (PILRalpha) 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 PILRalpha, 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 PILRalpha. 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 PILRalpha to gB.
Wang
Jing
J
Laboratory of Immunochemistry, WPI Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, Japan.
Fan
Qing
Q
Satoh
Takeshi
T
Arii
Jun
J
Lanier
Lewis L
LL
Spear
Patricia G
PG
Kawaguchi
Yasushi
Y
Arase
Hisashi
H
D006031:Glycosylation; D008562:Membrane Glycoproteins / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry*; D011971:Receptors, Immunologic / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism*
D008562:Membrane Glycoproteins; C412263:PILRA protein, human; D011134:Polysaccharides; D011971:Receptors, Immunologic; D014759:Viral Envelope Proteins; C040495:glycoprotein B, Simplexvirus