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

Abstract

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.

Ruminant alphaherpesviruses related to bovine herpesvirus 1

“…Generally, gE and gI seem to be important for BoHV-5 neuropathogenicity and its ability to reactivate from latency [53]. Glycoprotein H is one of the most conserved glycoproteins in herpesviruses [46]. BoHV-1 and BoHV-5 gH are both expressed as early-late proteins.…”

The Nucleotide Sequence of an Equine Herpesvirus 4 Gene Homologue of the Herpes Simplex Virus 1 Glycoprotein H Gene

“…EHV-4 and HSV-1 gHs and, indeed, throughout the alpha-, beta-and gammaherpesvirus gHs investigated implies some degree of conservation of the secondary and tertiary structure of these proteins presumably involving disulphide bonding (Gompels et al, 1988). The potential of gH to elicit antibody which can neutralize viral infectivity in the absence of complement suggests that the glycoprotein might be a useful constituent of a vaccine preparation.…”

“…With the exception of pseudorabies virus gH which is only 686 amino acids in length, the gHs of alphaherpesviruses tend to be larger than their beta-and gammaherpesvirus counterparts, ranging from 838 A comparison of the amino acid sequence of the gH proteins of alpha-, beta-and gammaherpesviruses by Gompels et al (1988) andCranage et al (1988) indicated this greater diversity of sequence in the N-terminal region of the protein and highlighted several features of the gH protein conserved throughout the herpesvirus family: firstly, an unusually short cytoplasmic domain of 14 or 15 amino acids in alphaherpesviruses and of seven or eight amino acids in beta-and gammaherpesviruses, secondly, four conserved cysteine residues at similar positions relative to the putative transmembrane domain and within conserved local sequence, and thirdly, a conserved glycosylation site sequence NGTV 13 to 18 amino acids N-terminal to the transmembrane domain.…”

Induction of protective immunity with antibody to herpes simplex virus type 1 glycoprotein H (gH) and analysis of the immune response to gH expressed in recombinant vaccinia virus

“…Glycoprotein H (gH) of herpes simplex virus type 1 (HSV-1) is one of three glycoproteins that are essential for virus viability in tissue culture (Cai et al, 1988 ;Ligas & Johnson, 1988;Desai et al, 1988), and homologues of this glycoprotein have been identified in members of all the herpesvirus subfamilies (Davison & Taylor, 1987;Gompels et al, 1988;Cranage et al, 1988;Heineman et al, 1988). gH is required for virus entry (Desai et al, 1988) and is probably involved in cell to cell spread of infectivity since gH-specific monoclonal antibodies (MAbs), in addition to neutralizing free virus, inhibit cell fusion by syncytial strains and prevent intercellular virus transmission (Buckmaster et al, 1984;Gompels & Minson, 1986).…”