Neutralization epitope of varicella zoster virus on native viral glycoprotein gp118 (VZV glycoprotein gplll)

Montalvo, Eduardo A.; Grose, Charles

doi:10.1016/0042-6822(86)90124-8

Cited by 57 publications

(56 citation statements)

References 33 publications

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“…Both these glycoproteins function in mediating virus infectivity but in the most characterized herpesvirus, HSV, it is gH rather than gB that acts as a major target for complement-independent antibody-mediated neutralization of virus infectivity and inhibition of cell-to-ceU spread (Buckmaster et al, 1984;Para et al, 1985;Gompels & Minson, 1986). These characteristics have also been observed for the gH homologue in VZV, gpIII (Grose et al, 1983 ;Forghani et al, 1984;Keller et al, 1984;Davison et al, 1986;Montalvo & Grose, 1986;Keller et al, 1987). Consistent with the results shown with antibodies are the studies with an HSV conditional lethal mutant, tsQ26 (Weller et al, 1983), which has a point mutation in the gH gene (Desai et al, 1988).…”

Section: Introductionmentioning

confidence: 53%

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: Introductionmentioning

confidence: 53%

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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“…The results also indicated that the antibody to gH, which has neutralizing activity, recognizes a conformational epitope (Forghani et al, 1994 ;Montalvo & Grose, 1986). The monoclonal antibody to gH neutralized VZV and blocked cellto-cell spread (Forghani et al, 1994 ;Montalvo & Grose, 1986 ;Sugano et al, 1991). The immune response to gH : gL was first recognized in the study of gB, gE : gI and gH : gL in guinea-pigs infected with the Oka varicella vaccine (Sato et al, Author for correspondence : Kimiyasu Shiraki.…”

mentioning

confidence: 98%

Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site

Yokoyama

Ayabe

Miyagi

et al. 2001

Journal of General Virology

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“…Moreover, these glycoproteins have been shown to be important determinants of virus infectivity (Forrester et al, 1991 ;Misra & Blewett, 1991 ;Cai et al, 1988;Cranage et al, 1988). Monoclonal antibodies to HSV-1 gH and its homologues in VZV, HCMV and EBV are strongly neutralizing, suggesting that gH represents a neutralizing target in all herpesviruses (Forrester et al, 1991 ;Cranage et al, 1988;Oba & Hutt-Fletcher, 1988;Montalvo & Grose, 1986;Rasmussen et al, 1984;Grose et al, 1983).…”

mentioning

confidence: 99%

Identification of the glycoprotein H gene of murine cytomegalovirus

Dallas

Lyons

et al. 1992

Journal of General Virology

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Neutralization epitope of varicella zoster virus on native viral glycoprotein gp118 (VZV glycoprotein gplll)

Cited by 57 publications

References 33 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

Varicella-zoster virus gH:gL contains a structure reactive with the anti-human gamma chain of IgG near the glycosylation site

Identification of the glycoprotein H gene of murine cytomegalovirus

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