Several herpesviruses induce expression of the
selectin receptor
sialyl-Lewis 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.