O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus

Johnson, David C.; Spear, Patricia G.

doi:10.1016/0092-8674(83)90083-1

Cited by 283 publications

(208 citation statements)

References 56 publications

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“…Thus, a subfraction of about 6~ of the glucosamine label of HPA-binding gC seemed to be located on HPA-binding oligosaccharides. These findings are consistent with reports that gC may contain N-linked as well as O-linked oligosaccharides (Olofsson et al, 1983;Johnson & Spear, 1983).…”

Section: Hpa-binding Oligosaccharides Of Hsv-1 Glycoprotein Csupporting

confidence: 82%

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Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides

Olofsson

Sjöblom

Lundström

et al. 1983

Journal of General Virology

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SUMMARYIn contrast to other viral glycoproteins, the herpes simplex virus (HSV) glycoprotein C (gC) binds to the N-acetylgalactosamine-specific Helix pomatia lectin (HPA). In the present paper gC was purified by affinity chromatography with monospecific antibodies and the purified glycoprotein was subjected to protease digestion. HPAbinding protease-resistant glycopeptides were isolated by lectin affinity chromatography. The isolated structures did not bind to concanavalin A and seemed to lack charged groups as determined by ion-exchange chromatography. In gel filtration, the glycopeptides appeared in two peaks with molecular weights higher than 4000. The HPA-binding structures of gC were synthesized in the presence of tunicamycin, indicating that they belong to the O-glycosyl class of oligosaccharides. In addition to HPA-binding oligosaccharides, synthesis of tunicamycin-resistant wheat germ lectinbinding gC oligosaccharides was demonstrable. These were sensitive to sialidase and apparently unrelated to the HPA-binding oligosaccharides.

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Section: Hpa-binding Oligosaccharides Of Hsv-1 Glycoprotein Csupporting

confidence: 82%

“…In contrast to these observations, Kumarasamy & Blough (1982) were unable to demonstrate a presence of O-linked glycans in gC. Johnson & Spear (1983) recently reported O-linked sialylated HSV oligosaccharides ranging from 1500 to 3000 mol. wt., i.e.…”

Section: Discussionmentioning

confidence: 72%

Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides

Olofsson

Sjöblom

Lundström

et al. 1983

Journal of General Virology

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“…Measurement of N-acetylgalactosaminyl : polypeptide transferase activity in subcellular fractions of hen oviduct (23), rat intestinal mucosa (33), and developing rat brain (34) showed presence of this enzyme in a smooth membrane fraction. Another line of evidence indicating that O-glycosylation takes place in smooth membrane fractions comes from recent work on viral glycoprotein maturation (29,40,60). In mammary gland explants, cycloheximide treatment inhibited immediately N-glycosylation, presumably due to lack of nascent polypeptide acceptors, whereas O-glycosylation continued for 30 min, a time period necessary for the movement of possible acceptor polypeptides from the rough endoplasmic reticulum 402 THE JOURNAL OF CELL BIOLOGY " VOLUME 98,1984 to the Golgi apparatus (71).…”

Section: Discussionmentioning

confidence: 99%

Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation.

Roth¹

1984

The Journal of Cell Biology

216

101

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The O-linked oligosaccharides of mucin-type glycoproteins contain N-acetyl-Dgalactosamine (GaINAc) that is not found in N-linked glycoproteins . Because Helix pornatia lectin interacts with terminal GaINAc, we used this lectin, bound to particles of colloidal gold, to localize such sugar residues in subcellular compartments of intestinal goblet cells. When thin sections of low temperature Lowicryl K4M embedded duodenum or colon were incubated with Helix pomatia lectin-gold complexes, no labeling could be detected over the cisternal space of the nuclear envelope and the rough endoplasmic reticulum . A uniform labeling was observed over the first and several subsequent cis Golgi cisternae and over the last (duodenal goblet cells) or the two last (colonic goblet cells) trans Golgi cisternae as well as forming and mature mucin droplets. However, essentially no labeling was detected over several cisternae in the central (medial) region of the Golgi apparatus . The results strongly suggest that core Oglycosylation takes place in cis Golgi cisternae but not in the rough endoplasmic reticulum . The heterogenous labeling for GaINAc residues in the Golgi apparatus is taken as evidence that termination of certain O-oligosaccharide chains by GaINAc occurs in trans Golgi cisternae .Glycoproteins can be classified according to the nature of the linkage between the oligosaccharide chains and the polypeptide. The two main families are those having oligosaccharide chains linked N-glycosidically from N-acetyl-D-glucosamine to the amide nitrogen of asparagine and those possessing oligosaccharide chains O-glycosidically linked from N-acetyl-D-galactosamine (GaINAc)' to the hydroxyl groups of serine and/or threonine (22,28,35,36,72). The biosynthesis of Nlinked glycoproteins is currently considered to be a single pathway involving the assembly ofa lipid linked oligosaccharide (1, 41, 42), the en bloc transfer of the oligosaccharide from the lipid carrier to the nascent peptide chain (31, 32, 55), the processing of the oligosaccharide chains by glycosidases (12,18,24,27,38,(63)(64)(65)(66)) and the addition of terminal sugars by glycosyltransferases (5, 44, 57). The establishment of the carbohydrate to protein linkage in N-glycosylation seems to be a cotranslational process located in the rough endoplasmic reticulum and later steps of the assembly are thought to occur mainly in the Golgi apparatus (2,22,28). Much less information is available about the assembly of the THE JOURNAL OF CELL BIOLOGY " VOLUME 98 FEBRUARY 1984 399-406 0The Rockefeller University Press -0021-9525/84/02/0399/08 $1 .00 oligosaccharide chains of O-linked glycoproteins and its topology . The initial glycosylation reaction in the synthesis of O-linked glycoproteins involves the direct transfer ofGaINAc from uridine diphosphate (UDP)-GaINAc to the polypeptide by a UDP-GaINAc: polypeptide transferase and does not require oligosaccharide preassembly nor lipid intermediates (22,23,25,36,37,58,67). Opinions vary among investigators, however, regarding the su...

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“…The antibiotic tunicamycin partially or completely blocks the glycosylation of glycoproteins by inhibiting the addition of highmannose N-linked oligosaccharides in the ER (Doms et al, 1993;Campadelli-Fiume & Serafini-Cessi, 1985), while the ionophore monensin, which interferes with Golgi function, blocks both the processing of N-linked oligosaccharides and the addition of O-linked oligosaccharides to HSV-1 glycoproteins (Johnson & Spear, 1983;Spear, 1985). Fig.…”

Section: Effect Of Glycosylation On Cleavage Of Ehv-1 Gbmentioning

confidence: 99%

N-terminal sequence analysis of equine herpesvirus 1 glycoproteins D and B and evidence for internal cleavage of the gene 71 product

Wellington

Gooley

Love

et al. 1996

Journal of General Virology

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Signal cleavage sites of equine herpesvirus 1 (EHV-1) glycoproteins D and B (gD and gB) and an endoproteolytic cleavage site of EHV-1 gB were determined by N-terminal amino acid sequencing and compared with known cleavage sites of homologues in other herpesviruses. Signal cleavage of EHV-1 gD occurred between Arg 35 and Ala 36 in a region of basic amino acids resembling the endoproteolytic cleavage sites of viral glycoproteins, nine amino acids downstream of the predicted site, while EHV-1 gB was cleaved as predicted between Ala s5 and Val s~. Endoproteolytic cleavage of EHV-1 gB occurred between Arg 54s and Ala 5aa, 28 amino acids downstream of the cleavage site predicted from conserved sequences of other herpesvirus gB homologues. One interpretation of these data is that EHV-1 gB is cleaved internally at both sites, a possibility which was supported by the apparent molecular masses of the unglycosylated gB subunits produced in the presence of tunicamycin. This double cleavage would release a stretch of amino acids which is not present in sequenced gB molecules of other herpesviruses. Experiments with glycosylation inhibitors indicated that cleavage of EHV-1 gB can occur in the absence of glycosylation. N-terminal sequencing also determined that a 42 kDa EHV-1 glycoprotein was a product of internal cleavage of the protein encoded by gene 71. Staggered endoproteolytic cleavage after adjacent arginine residues 506 and 507 separates the 42 kDa Cterminal subunit containing all the cysteine residues from the serine and threonine rich N-terminal region.

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O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus

Cited by 283 publications

References 56 publications

Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides

Glycoprotein C of Herpes Simplex Virus Type 1: Characterization of O-linked Oligosaccharides

Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation.

N-terminal sequence analysis of equine herpesvirus 1 glycoproteins D and B and evidence for internal cleavage of the gene 71 product

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