Glycosylation pathways of two major Epstein-Barr virus membrane antigens

Strnad, Bruce C.; Adams, Michael R.; Rabin, Harvey

doi:10.1016/0042-6822(83)90381-1

Cited by 22 publications

(19 citation statements)

References 25 publications

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“…Using the rules of von Heijne (1986), both sequences have predicted signal sequences of 16 and 17 residues, which may be cleaved to give proteins of Mr 80859 and 76403, respectively. All five sites for N-linked glycosylation in EBV gH (Strnad et al, 1983) are conserved in position in HVS gH. Two of these sites are also conserved in sequence, one towards the N terminus (WREANVTE) and one towards the C terminus, 11 to 13 residues before the proposed transmembrane sequences, in the motif NGTV.…”

Section: Similarity Of the Hvs Gh Gene To Homologous Genes From Humanmentioning

confidence: 95%

Conservation of Glycoprotein H (gH) in Herpesviruses: Nucleotide Sequence of the gH Gene from Herpesvirus Saimiri

Gompels¹,

Craxton²,

Honess³

1988

Journal of General Virology

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SUMMARYWe present the nucleotide sequence of the glycoprotein H (gH) gene of herpesvirus saimiri (HVS), a representative of the T lymphotropic herpesviruses of New World monkeys, and compare the predicted amino acid sequence with sequences of homologous proteins from four human herpesviruses. The HVS gH gene is located within a block of genes encoding products conserved in all herpesvirus subgroups as represented by the human herpesviruses herpes simplex virus, varicella-zoster virus, cytomegalovirus and Epstein-Barr virus. In agreement with the biological grouping of HVS as a lymphotropic gammaherpesvirus, its gH amino acid sequence shows greatest similarity to that of the B lymphotropic Epstein-Barr virus, although the nucleotide sequences of their respective gH genes show little similarity given different G +C compositions of 31~ and 54~. The similarity observed between the gH amino acid sequences of the two representative gammaherpesviruses is greater than that between the two human alphaherpesviruses varicella-zoster virus and herpes simplex virus. The members of the gH family range in size from 706 to 743 amino acid residues for the beta-and gammaherpesviruses, to 838 to 841 for the alphaherpesviruses, giving nonglycosylated precursors with Mr values of 78 322 to 93 651. The difference in size is due to heterogeneity in the poorly conserved N-terminal regions of the larger alphaherpesviruses compared to the smaller beta-and gammaherpesvirus molecules. Greatest similarity is observed in the C-terminal halves of the proteins including residues surrounding four conserved cysteine residues, a conserved N-linked glycosylation site (within the sequence NGTV) 13 to 18 residues proximal to the membrane-spanning sequences, and a short cytoplasmic domain of seven or eight residues for the beta-and gammaherpesviruses' and 14 or 15 residues for the alphaherpesviruses' gH. Thus, the representatives of all subgroups of herpesviruses, including those with a non-human host, encode gH homologues. Together with the observation that gH of these viruses are major targets for virus neutralization by antibody, this suggests that this glycoprotein family is essential among all herpesviruses and represents a major component involved in herpesvirus infectivity.

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Section: Similarity Of the Hvs Gh Gene To Homologous Genes From Humanmentioning

confidence: 95%

Conservation of Glycoprotein H (gH) in Herpesviruses: Nucleotide Sequence of the gH Gene from Herpesvirus Saimiri

Gompels¹,

Craxton²,

Honess³

1988

Journal of General Virology

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“…EBV-MA consists of the glycoproteins gp350 and gp220 that are encoded by the same gene, which has been mapped to the BamHI L DNA fragment of the B95-8 genome [6]. The mRNA of gp220 arises by internal splicing of the mRNA of gp350 in such a manner that the same open reading frame (BLLFl) is maintained [6].…”

Section: Introductionmentioning

confidence: 99%

“…The mRNA of gp220 arises by internal splicing of the mRNA of gp350 in such a manner that the same open reading frame (BLLFl) is maintained [6]. EBV-MA is important for virion binding to human B lymphocytes via its specific in- [19].…”

Section: Introductionmentioning

confidence: 99%

Purification and quantification of recombinant Epstein-Barr viral glycoproteins gp350/220 from Chinese hamster ovary cells

Hessing¹,

Schijndel²,

Grunsven³

et al. 1992

Journal of Chromatography A

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“…Both proteins are heavily glycosylated with > 50 % of their M r due to carbohydrate (Edson & Thorley-Lawson, 1983). Oligosaccharides on gp350 are both N-and O-linked (Serafini-Cessi et al, 1989;Gong & Kieff, 1990) and glycosylation is blocked by tunicamycin (Edson & Thorley-Lawson, 1981Strnad et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

Conformation-dependent recognition of baculovirus-expressed Epstein--Barr virus gp350 by a panel of monoclonal antibodies

Zhang

Marcus-Sekura²

1993

Journal of General Virology

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Glycosylation pathways of two major Epstein-Barr virus membrane antigens

Cited by 22 publications

References 25 publications

Conservation of Glycoprotein H (gH) in Herpesviruses: Nucleotide Sequence of the gH Gene from Herpesvirus Saimiri

Conservation of Glycoprotein H (gH) in Herpesviruses: Nucleotide Sequence of the gH Gene from Herpesvirus Saimiri

Purification and quantification of recombinant Epstein-Barr viral glycoproteins gp350/220 from Chinese hamster ovary cells

Conformation-dependent recognition of baculovirus-expressed Epstein--Barr virus gp350 by a panel of monoclonal antibodies

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