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pubmed-article:19812165pubmed:abstractTextPaired 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.lld:pubmed
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pubmed-article:19812165pubmed:authorpubmed-author:SpearPatricia...lld:pubmed
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pubmed-article:19812165pubmed:authorpubmed-author:SatohTakeshiTlld:pubmed
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pubmed-article:19812165pubmed:authorpubmed-author:WangJingJlld:pubmed
pubmed-article:19812165pubmed:authorpubmed-author:FanQingQlld:pubmed
pubmed-article:19812165pubmed:authorpubmed-author:AriiJunJlld:pubmed
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pubmed-article:19812165pubmed:volume83lld:pubmed
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pubmed-article:19812165pubmed:pagination13042-5lld:pubmed
pubmed-article:19812165pubmed:dateRevised2010-9-27lld:pubmed
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pubmed-article:19812165pubmed:articleTitleBinding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor alpha depends on specific sialylated O-linked glycans on gB.lld:pubmed
pubmed-article:19812165pubmed:affiliationLaboratory of Immunochemistry, WPI Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, Japan.lld:pubmed
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pubmed-article:19812165pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
pubmed-article:19812165pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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