Characterization of N- and O-linked oligosaccharides of glycoprotein 350 from Epstein-Barr virus

Serafini‐Cessi, Franca; Malagolini, Nadia; Nanni, M.; Dall’Olio, Fabio; Campadelli-Fiume, Gabriella; Tanner, Jerome E.; Kieff, Elliott

doi:10.1016/0042-6822(89)90345-0

Cited by 28 publications

(15 citation statements)

References 40 publications

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“…Many other herpesvirus glycoproteins have been shown to be partly composed of O-linked carbohydrate, such as HSV-1 gB, gC, gD and gE (Johnson & Spear, 1983;Olofsson et al, 1983;Wenske & Courtney, 1983;Serafini-Cessi et al, 1988), but this is of low abundance in comparison with N-linked carbohydrate. The EBV gp350 has approximately 50~ of its carbohydrate present as O-linkages (Serafini-Cessi et al, 1989), but the only characterized alphaherpesvirus glycoprotein in which O-linked carbohydrate predominates is HSV-2 gG (Serafini-Cessi et al, 1985), which has approximately 25 times as much carbohydrate present in the O-linkage form than in the N-linkage form. The EBV gp350 has been shown to have homology to HSV-1 gC (Tanner et al, 1987) but, because a gC homologue in EHV-1 has already been identified (Allen & Coogle, 1988;Guo et al, 1989), a relationship here is unlikely.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the high Mr glycoprotein (gP300) of equine herpesvirus type 1 as a novel glycoprotein with extensive O-linked carbohydrate

Whittaker

Wheldon²,

Giles³

et al. 1990

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

Characterization of the high Mr glycoprotein (gP300) of equine herpesvirus type 1 as a novel glycoprotein with extensive O-linked carbohydrate

Whittaker

Wheldon²,

Giles³

et al. 1990

Journal of General Virology

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“…1C). Although dispensable for infectivity, gp350 is important for the initial attachment to B cells (80) and has been shown to be highly O-glycosylated (81). gp350 also represents a very potent immunogen (82,83).…”

Section: Mapping O-glycosites In Human Herpesvirusesmentioning

confidence: 99%

Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

Bagdonaite

Nordén

Joshi

et al. 2016

Journal of Biological Chemistry

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Herpesviruses are among the most complex and widespread viruses, infection and propagation of which depend on envelope proteins. These proteins serve as mediators of cell entry as well as modulators of the immune response and are attractive vaccine targets. Although envelope proteins are known to carry glycans, little is known about the distribution, nature, and functions of these modifications. This is particularly true for O-glycans; thus we have recently developed a "bottom up" mass spectrometry-based technique for mapping O-glycosylation sites on herpes simplex virus type 1. We found wide distribution of O-glycans on herpes simplex virus type 1 glycoproteins and demonstrated that elongated O-glycans were essential for the propagation of the virus. Here, we applied our proteome-wide discovery platform for mapping O-glycosites on representative and clinically significant members of the herpesvirus family: varicella zoster virus, human cytomegalovirus, and Epstein-Barr virus. We identified a large number of O-glycosites distributed on most envelope proteins in all viruses and further demonstrated conserved patterns of O-glycans on distinct homologous proteins. Because glycosylation is highly dependent on the host cell, we tested varicella zoster virus-infected cell lysates and clinically isolated virus and found evidence of consistent O-glycosites. These results present a comprehensive view of herpesvirus O-glycosylation and point to the widespread occurrence of O-glycans in regions of envelope proteins important for virus entry, formation, and recognition by the host immune system. This knowledge enables dissection of specific functional roles of individual glycosites and, moreover, provides a framework for design of glycoprotein vaccines with representative glycosylation.

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“…BILF2 encodes gp78/55, an N-linked glycoprotein, and also is detectable in the envelope of EBV virions (29,47). gp350/220 are the products of BLLF1, and these N-and O-linked glycoproteins are the most abundant components of the EBV envelope and important for host cell receptor binding and host cell invasion (52,61). BLRF2 encodes a tegument protein, p23 (60).…”

Section: Discussionmentioning

confidence: 99%

Role of the TSG101 Gene in Epstein-Barr Virus Late Gene Transcription

Chua

Lee

Chang

et al. 2007

J Virol

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Characterization of N- and O-linked oligosaccharides of glycoprotein 350 from Epstein-Barr virus

Cited by 28 publications

References 40 publications

Characterization of the high Mr glycoprotein (gP300) of equine herpesvirus type 1 as a novel glycoprotein with extensive O-linked carbohydrate

Characterization of the high Mr glycoprotein (gP300) of equine herpesvirus type 1 as a novel glycoprotein with extensive O-linked carbohydrate

Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus

Role of the TSG101 Gene in Epstein-Barr Virus Late Gene Transcription

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