Altered Kinetic Properties of Sialyl and Galactosyl Transferases Associated with Herpes Simplex Virus Infection of GMK and BHK Cells

Abstract

SUMMARYMicrosomal sialyl transferase and galactosyl transferase activities of herpes simplex virus-infected GMK and BHK cells were studied. Apparent Km values calculated for sialyl and galactosyl transferases differed significantly from the corresponding values of uninfected cells. Both transferases of HSV-infected cells demonstrated accepter specificities different from those of uninfected cells. It is suggested that herpes simplex virus might influence glycosylation of proteins by modifying the glycosyl transferases of the infected cells.

Dendritic cells mediate herpes simplex virus infection and transmission through the C-type lectin DC-SIGN

“…Thus, differences in the cell type and method of production might account for the differences observed. Indeed, infection by HSV-1 induces glycosylation changes (Olofsson et al, 1980;Nystrom et al, 2004) and insect cells lack the glycosylation components necessary to generate glycosylations present in eukaryotic cells (Altmann et al, 1999). Thus, gB and gC produced in eukaryotic cells represent the glycosylations observed in HSV-1 particles, which are recognized by DC-SIGN.…”

The Lipoxin Receptor ALX: Potent Ligand-Specific and Stereoselective Actions in Vivo

“…Conserved N-glycosylation sites are present on Asn-4 and Asn-179 of human ALX. Bacterial and viral infections interfere with normal N-glycosylation of the host cells (Olofsson et al, 1980;Kim and Cunningham, 1993;Villanueva et al, 1994), and this characteristic of the ALX receptor for ligand class recognition was of interest to assess. In this regard, deglycosylation of ALX does not dramatically alter LXA 4 recognition, but significantly lowers the affinity for ALX peptide ligands (i.e., MMK-1 and MHC binding peptide) .…”

Aminosugar derivatives as potential anti-human immunodeficiency virus agents.

“…Consequently, the hostcell glycosylation apparatus must be used to generate virions expressing species-specific and cell-type-specific oligosaccharides on the envelope glycoprotein. However, the finding that some viruses use posttranslational glycosylation (18) (i.e., not cotranslational) transfer to protein of nonglucosylated oligomannose oligosaccharides (8) or modify the kinetic properties of cellular sialyl-and galactosyltransferases (19) suggest that viruses might code for nonstructural factors. At present it is not known whether viral surface glycoproteins already embedded in the outer cell membrane before viral budding begins supply viral assembly (i.e., the biosynthesis of the ellipsoid glycoprotein knobs of HIV) (5).…”