Domains of Virus Glycoproteins

Schlesinger, Milton J.; Schlesinger, Sondra

doi:10.1016/s0065-3527(08)60315-2

Cited by 34 publications

(28 citation statements)

References 168 publications

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“…The 717 amino acid sequence encoded by the HVS gH gene shows characteristics predictive of a membrane-spanning glycoprotein; these include hydrophobic signal and transmembrane sequences, a positively charged cytoplasmic anchor sequence, and the presence of N-linked glycosylation sites (Schlesinger & Schlesinger, 1987 ;Kornfeld & Kornfeld, 1985 ;Walter et al, 1984;Eisenberg, 1984). In Fig.…”

Section: Dna Sequence Analysismentioning

confidence: 99%

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: Dna Sequence Analysismentioning

confidence: 99%

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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“…2). It has many of the characteristics of a transmembrane glycoprotein (Schlesinger & Schlesinger, 1987;Eisenberg, 1984): there are eight potential sites (NXT/S) for N-linked glycosylation, an N-terminal hydrophobic sequence which may serve as a signal sequence, a C-terminal hydrophobic region which may act as a transmembrane anchor sequence, and a positively charged cytoplasmic anchor sequence of seven amino acids at the C terminus (Fig. 2).…”

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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“…This pH-dependent cell fusion event is likely mediated by gp43 since it is the only membrane-anchored GP species found on the plasma membrane. In addition, gp43 contains a hydrophobic sequence near its N terminus that has features similar to those of the fusogenic peptide sequences described for paramyxoviruses and influenza virus (42). However, the domains of BDV GP involved in receptor recognition and cell entry have not been defined.…”

mentioning

confidence: 99%

N-Terminal Domain of Borna Disease Virus G (p56) Protein Is Sufficient for Virus Receptor Recognition and Cell Entry

Perez

Watanabe

Whitt

et al. 2001

J Virol

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Borna disease virus (BDV) surface glycoprotein (GP) (p56) has a predicted molecular mass of 56 kDa. Due to extensive posttranslational glycosylation the protein migrates as a polypeptide of 84 kDa (gp84). The processing of gp84 by the cellular protease furin generates gp43, which corresponds to the C-terminal part of gp84. Both gp84 and gp43 have been implicated in viral entry involving receptor-mediated endocytosis and pH-dependent fusion. We have investigated the domains of BDV p56 involved in virus entry. For this, we used a pseudotype approach based on a recently developed recombinant vesicular stomatitis virus (VSV) in which the gene for green fluorescent protein was substituted for the VSV G protein gene (VSV⌬G*). Complementation of VSV⌬G* with BDV p56 resulted in infectious VSV⌬G* pseudotypes that contained both BDV gp84 and gp43. BDV-VSV chimeric GPs that contained the N-terminal 244 amino acids of BDV p56 and amino acids 421 to 511 of VSV G protein were efficiently incorporated into VSV⌬G* particles, and the resulting pseudotype virions were neutralized by BDV-specific antiserum. These findings indicate that the N-terminal part of BDV p56 is sufficient for receptor recognition and virus entry.Borna disease virus (BDV) is the causal agent of Borna disease, a frequently fatal meningoencephalitis affecting mainly horses and sheep in certain regions of central Europe. Experimentally, BDV can infect a remarkably large number of vertebrate species. The infection is characterized by a variable period of incubation with diverse clinical and pathological manifestations (15,25,37), and behavioral disturbances are a hallmark of BDV infection. Serological and molecular-epidemiology data indicate that the host range, geographic distribution, and prevalence of BDV may be much broader than previously thought. There is also evidence that BDV can infect humans and might be associated with some neuropsychiatric disorders (1,2,9,10,18,24,28,30,38,41). However, the prevalence and possible clinical significance of BDV in humans remain controversial (46).BDV is an enveloped, nonsegmented, negative-strand (NNS) RNA virus (8,43). BDV has the smallest genome size, 8.9 kb, among known mononegaviruses. Unlike what is found for all other NNS RNA animal viruses, transcription and replication of the BDV genome take place in the nucleus (3-5). BDV uses RNA splicing for the regulation of its genome expression, which is also unique among known mononegaviruses. Based on its unique biological and molecular-genetics features, BDV is now considered to be the prototypic member of a new family, Bornaviridae, within the order Mononegavirales.The BDV genome contains six major open reading frames (ORFs). The product of BDV ORF IV is the counterpart of the type I surface glycoproteins (GPs) found in other members of the Mononegavirales. BDV GP (p56) has a predicted molecular mass of 56 kDa, but due to extensive N glycosylation the protein migrates with an apparent molecular mass of 84 kDa (gp84). BDV GP is processed posttranslationally by the su...

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Domains of Virus Glycoproteins

Cited by 34 publications

References 168 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

Identification of the glycoprotein H gene of murine cytomegalovirus

N-Terminal Domain of Borna Disease Virus G (p56) Protein Is Sufficient for Virus Receptor Recognition and Cell Entry

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