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Involvement of viral glycoprotein gC ‐1 in expression of the selectin ligand sialyl‐Lewis X induced after infection with herpes simplex virus type 1
Author(s) -
Nordén Rickard,
Nyström Kristina,
Adamiak Beata,
Halim Adnan,
Nilsson Jonas,
Larson Göran,
Trybala Edward,
Olofsson Sigvard
Publication year - 2013
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1600-0463.2012.02967.x
Subject(s) - glycoprotein , herpes simplex virus , mucin , fucosyltransferase , glycan , glycolipid , biology , sialyl lewis x , microbiology and biotechnology , glycoconjugate , mutant , fucosylation , herpesvirus glycoprotein b , virus , virology , chemistry , gene , viral entry , viral replication , biochemistry , selectin , cell adhesion molecule
Several herpesviruses induce expression of the selectin receptor sialyl‐ L ewis X (sLe x ) by activating transcription of one or more of silent host FUT genes, each one encoding a fucosyltransferase that catalyses the rate‐limiting step of sLe x synthesis. The aim here was to identify the identity of the glycoconjugate associated with sLe x glycoepitope in herpes simplex virus type 1 ( HSV ‐1) infected human diploid fibroblasts, using immunofluorescence confocal microscopy. Cells infected with all tested HSV ‐1 strains analysed demonstrated bright sLe x fluorescence, except for two mutant viruses that were unable to induce proper expression of viral glycoprotein gC ‐1: One gC ‐1 null mutant and another mutant expressing gC ‐1 devoid of its major O‐glycan‐containing region (aa 33–116). The sLe x reactivity of HSV ‐1 infected cells was abolished by mild alkali treatment. Altogether the results indicated that the detectable sLe x was associated with O ‐linked glycans, situated in the mucin region of gC ‐1. No evidence for sLe x (i) in other HSV ‐1 glycoproteins with mucin domains such as gI‐1 or (ii) in host cell glycoproteins/glycolipids was found. Thus, the mucin domain of HSV ‐1 gC ‐1 may support expression of selectin ligands such as sLe x and other larger O ‐linked glycans in cell types lacking endogenous mucin domain‐containing glycoproteins, optimized for O ‐glycan expression, provided that the adequate host glycosyltransferase genes are activated.