N-acetylgalactosaminyltransferase activity involved in O-glycosylation of herpes simplex virus type 1 glycoproteins

Serafini‐Cessi, Franca; Dall’Olio, Fabio; Scannavini, M; Costanzo, F.; Campadelli-Fiume, Gabriella

doi:10.1128/jvi.48.1.325-329.1983

Cited by 18 publications

(7 citation statements)

References 30 publications

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“…Similarly, other mucin-like region-containing proteins such as HSV-1 gI, HSV-2 gG, EBV gp150 and gp350 have been shown to accommodate high density of O-glycosylation, and the types of O-glycan structures were identified for some of these proteins Nolan and Morgan 1995;Borza and Hutt-Fletcher 1998;Norberg et al 2007). The conserved viral fusion effector gB has been shown or predicted to be O-glycosylated in all herpesvirus subfamilies (Serafini-Cessi, Dall'Olio, Scannavini, Costanzo et al 1983;Gong et al 1987;Montalvo and Grose 1987;Britt and Vugler 1989). The era of proteome-wide mass spectrometry-based applications allowed robust characterization of viral O-glycoproteomes (Bagdonaite et al 2015Iversen et al 2016).…”

Section: Global O-glycoproteomicsmentioning

confidence: 99%

Global aspects of viral glycosylation

2018

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Enveloped viruses encompass some of the most common human pathogens causing infections of different severity, ranging from no or very few symptoms to lethal disease as seen with the viral hemorrhagic fevers. All enveloped viruses possess an envelope membrane derived from the host cell, modified with often heavily glycosylated virally encoded glycoproteins important for infectivity, viral particle formation and immune evasion. While N-linked glycosylation of viral envelope proteins is well characterized with respect to location, structure and site occupancy, information on mucin-type O-glycosylation of these proteins is less comprehensive. Studies on viral glycosylation are often limited to analysis of recombinant proteins that in most cases are produced in cell lines with a glycosylation capacity different from the capacity of the host cells. The glycosylation pattern of the produced recombinant glycoproteins might therefore be different from the pattern on native viral proteins. In this review, we provide a historical perspective on analysis of viral glycosylation, and summarize known roles of glycans in the biology of enveloped human viruses. In addition, we describe how to overcome the analytical limitations by using a global approach based on mass spectrometry to identify viral O-glycosylation in virus-infected cell lysates using the complex enveloped virus herpes simplex virus type 1 as a model. We underscore that glycans often pay important contributions to overall protein structure, function and immune recognition, and that glycans represent a crucial determinant for vaccine design. High throughput analysis of glycosylation on relevant glycoprotein formulations, as well as data compilation and sharing is therefore important to identify consensus glycosylation patterns for translational applications.

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Section: Global O-glycoproteomicsmentioning

confidence: 99%

Global aspects of viral glycosylation

2018

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“…Most likely, Nglycanase is cleaving all N-linkages (71) and leaving 0-linked sugars, whereas tunicamycin treatment is blocking all cotranslational or posttranslational modifications of gpllO by blocking formation of dolichol phosphate intermediates and thereby preventing transfer of the nascent polypeptide to the golgi (24,70,73). Further, it is known that HSV gB contains both N-and 0-linked glycosylation (36,43,51,64). Also, tunicamycin treatment of EBV-infected cells results in a 135-kDa cross-reactive putative precursor to EBV gp350, which is identical in size to the in vitro translation product of gp350 mRNA (34).…”

Section: -mentioning

confidence: 99%

Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB

Gong¹,

Ooka²,

Matsuo³

et al. 1987

J Virol

103

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, has now been shown to encode a 110-kilodalton glycoprotein. Late infectious cycle RNAs of 3.0 and 1.8 kilobases are transcribed from BALF4. Translation of these RNAs in vitro, transcription and translation of BALF4 in vitro, or metabolic labeling of cells in the presence of tunicamycin and immunoprecipitation with BALF4-specific sera results in identification of a 93-kilodalton precursor to gpllO. Since N-glycosidase F only reduces the size of gpllO to 105 kilodaltons, gpllO probably has both N-and 0-linked glycosylation. gpllO is an abundant glycoprotein in Epstein-Barr virus-infected cells. In infected lymphocytes and in 3T3 cells, in which the gene is expressed from a recombinant expression vector, most of the protein is cytoplasmic and perinuclear. In contrast to gB, gpllO was not detected in the infected-cell plasma membrane. In cells replicating Epstein-Barr virus, gpllO localized to the inner and outer nuclear membrane lamellae and to endoplasmic reticulum structures which sometimes contained enveloped virus. gpllO may play an important role in modifying infected intracellular membranes.

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“…Previously we reported the occurrence in HSV-1-infected BHK cells of N-acetylgalactosaminyltransferase, which catalyzes in vitro the addition of GalNAc to hyroxyamino acids of immature forms of HSV-1 glycoproteins, including immature gC (27). The inability of the mature forms of HSV-1 glycoproteins to accept in vitro GalNAc was related to the inadequate configuration of mature glycoproteins, which carry fully processed oligosaccharides.…”

Section: Species the Percentage Distribution Of Radioactive Glcn Andmentioning

confidence: 99%

Sialylated oligosaccharides O-glycosidically linked to glycoprotein C from herpes simplex virus type 1

Dall’Olio¹,

Malagolini²,

Speziali³

et al. 1985

J Virol

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Glycoprotein C (gC) was purified by immunoabsorbent from herpes simplex virus type-1-infected BHK cells labeled with [14C]glucosamine for 11 h and chased for 3 h. Glycopeptides obtained by pronase digestion of gC were fractionated by Bio-Gel filtration and concanavalin A-Sepharose chromatography. Each glycopeptide fraction was analyzed for amino sugar composition by thin-layer chromatography. The majority of radioactivity was recovered as N-acetylglucosamine, but a significant amount of labeled N-acetylgalactosamine was detected and recovered preferentially in some glycopeptide species. Mild alkaline borohydride treatment of the glycopeptides resulted in the release of small degradation products which contained N-acetylgalactosaminitol as the major labeled component and a drastic reduction of N-acetylgalactosamine in the residual glycopeptides. These results demonstrated that gC carries 0-glycosidically linked oligosaccharides in addition to the N-linked di-and triantennary glycans previously described (F. Serafini-Cessi, F. Dall'Olio, L. Pereira, and G. Campadelli-Fiume, J. Virol. 51:838-844, 1984). Chromatographic behavior on DEAE-Sephacel chromatography and neuraminidase digestion of 0-linked oligosaccharides indicated the presence of two major sialylated species carrying one and two sialic acid residues, respectively. The characterization of a peculiar glycopeptide species supported the notion that some of the 0-linked oligosaccharides are bound to a cluster of hydroxyamino acids located near an N-glycosylation site which carries one N-linked diantennary oligosaccharide.

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N-acetylgalactosaminyltransferase activity involved in O-glycosylation of herpes simplex virus type 1 glycoproteins

Cited by 18 publications

References 30 publications

Global aspects of viral glycosylation

Global aspects of viral glycosylation

Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB

Sialylated oligosaccharides O-glycosidically linked to glycoprotein C from herpes simplex virus type 1

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