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
Year: 2009
Type: article
Abstract: 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.
Source: Journal of Virology
DOI: 10.1128/jvi.00792-09
Authors: Jing Wang, Qing Fan, Takeshi Satoh, Jun Arii, Lewis L. Lanier, Patricia G. Spear, Yasushi Kawaguchi, Hisashi Arase
Language: English
Subfield: Epidemiology
Field: Medicine
Domain: Health Sciences
Open Access status: green
Awards: G1441504317, G4388675607, G6581122219
OpenAlex ID: W2154401381
