Herpes Simplex Virus Type-1 Glycoprotein D Gene: Nucleotide Sequence and Expression in
            <i>Escherichia coli</i>

Watson, Roger J.; Weis, John H.; Salstrom, John S.; Enquist, Lynn W.

doi:10.1126/science.6289440

Cited by 257 publications

(183 citation statements)

References 23 publications

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“…Its 316-aa ectodomain has three N-glycosylation sites and six cysteine residues forming three disulfide bonds (9,10). X-ray structures have been reported for a truncated form of the HSV-1 gD ectodomain (first 285 aa), crystallized alone and in complex with HVEM (7).…”

Section: E Nveloped Viruses Of Humans and Animals Invade Cells By Induc-mentioning

confidence: 99%

Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion

Zago

Jogger

Spear

2004

Proc. Natl. Acad. Sci. U.S.A.

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Membrane fusion induced by herpes simplex virus (HSV) requires the action of four viral membrane glycoproteins (gB, gD, gH, and gL) and the binding of gD to one of its receptors, such as the herpesvirus entry mediator or nectin-1. The related animal herpesvirus, pseudorabies virus (PRV), encodes a homologous set of glycoproteins and its gD can also use nectin-1 as an entry receptor. We show here that PRV gD, when coexpressed with HSV gB, gH, and gL, cannot substitute for HSV gD in inducing fusion with target cells expressing nectin-1. Chimeric gD molecules composed of HSV and PRV sequences can substitute, provided the first 285 aa are from HSV gD. Because the first 261 aa were sufficient for receptor binding, this suggested that amino acids 262-285 contain a region required for cell fusion but not for receptor binding. Deletions from amino acids 250 -299 failed to identify a specific subregion critical for cell fusion, except possibly for amino acids 250 -255, which also influenced receptor binding. Instead, presence of a flexible stalk between the membrane and receptor-binding domain appears to be required, perhaps to enable conformational changes in gD on receptor binding and subsequent interactions of undefined regions of gD with the other glycoproteins required for membrane fusion. E nveloped viruses of humans and animals invade cells by inducing fusion between the viral envelope and a cell membrane. Viral envelope glycoproteins initiate and mediate this fusion. In some cases, a single viral glycoprotein can mediate binding of virus to the cell surface and fusion with a cell membrane. In other cases, two viral glycoproteins or subunits of a single translation product are required for binding and fusion (reviewed in ref. 1). In the case of herpes simplex virus (HSV), four distinct glycoproteins (gB, gD, gH, and gL) are required for membrane fusion, whereas the initial attachment of virus to cell can be mediated by gB or gC binding to cell surface heparan sulfate (reviewed in refs. 2 and 3). The initiation of membrane fusion requires the interaction of gD with one of its receptors. These include the herpesvirus entry mediator (HVEM); nectin-1 and nectin-2, cell adhesion molecules in the Ig superfamily; and specific sites in heparan sulfate generated by particular 3-O-sulfotransferases (reviewed in ref. 4).It remains unclear why HSV, and herpesviruses in general, require multiple envelope glycoproteins to induce membrane fusion. It seems unlikely that gD is an actual fusogen. All known viral fusogens must be anchored to the viral envelope as a transmembrane protein, whereas a glycosylphosphatidylinositol-linked gD ectodomain is functional for cell fusion (5) and soluble forms of the gD ectodomain can complement the entry defect of a gD-negative HSV (6). It has been proposed that interactions of gD with one of its receptors causes conformational changes in gD that enable it to activate the fusogenic activity of gB, a homooligomer, and͞or gH-gL, a heterodimer (6-8).HSV-1 gD is a 369-residue type 1 membrane glycop...

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Section: E Nveloped Viruses Of Humans and Animals Invade Cells By Induc-mentioning

confidence: 99%

Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion

Zago

Jogger

Spear

2004

Proc. Natl. Acad. Sci. U.S.A.

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“…The sequence spanned the gB gene which is transcribed from right to left in the prototypic form of the viral genome. The XhoISphI sites used to excise the structural gene from an EcoRI-F clone are indicated and the fragment generated contains the coding region and polyadenylation signal, (b) HSV-1 strain Patton (Watson et al, 1982) was sequenced between 0.90 and 0.93 m.u. of the Us region, spanning the 5' non-coding and coding regions of the gD gene.…”

Section: Cloning the Structural Genes For Hsv-1 Gb And Gdmentioning

confidence: 99%

“…The published sequence of gD-1 (strain Patton : Watson et al, 1982) was used to choose suitable restriction sites to excise the structural gene of gD-1 (strain Patton) from a BamHI-J clone. The 5' and 3' restriction sites chosen were the HindIII and NruI sites respectively (Fig.…”

Section: Cloning the Structural Genes For Hsv-1 Gb And Gdmentioning

confidence: 99%

Specificity of the Immune Response of Mice to Herpes Simplex Virus Glycoproteins B and D Constitutively Expressed on L Cell Lines

Blacklaws

Nash

Darby

1987

Journal of General Virology

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SUMMARYMouse L cell lines have been developed which constitutively express glycoproteins B (gB) and D (gD) of herpes simplex virus type 1. When used to study the immune response of mice to the viral glycoproteins, it was found that both gB and gD induce a delayed type hypersensitivity response and both also induce an antibody response, but only the cell line expressing gD could stimulate the production of neutralizing antibody. Virus-specific cytotoxic T lymphocytes (CTLs) recognized gB expressed by the cell line and this line could also induce CTLs in mice. Recognition of gD by major histocompatibility complex class I restricted CTLs was never seen. Vaccination of mice with the cell lines provided protection from viral challenge and inhibited the establishment of a latent infection, although gD proved to be the better protective immunogen. INTRODUCTIONThe immune response of mice to herpes simplex virus type 1 (HSV-1) is known to involve both antibody and cell-mediated protective mechanisms. In particular, T lymphocytes are considered to play a central role in the recovery from a primary infection (for review, see Nash et al., 1985). However, the particular proteins of the virus recognized by these cells are far from clear. Experiments to date have centred on the use of the virus mutants deficient in the expression of certain glycoproteins to study the nature of the antigens recognized by cytotoxic T lymphocytes (CTLs) (Carter et al., 1981;Lawman et al., 1980;Glorioso et al., 1985), and the affinity purification of glycoproteins from whole virus preparations for use as immunogens to study delayed type hypersensitivity (DTH) responses (Schrier et al., 1983;Chan et al., 1985).The main problem has been how to separate the various antigens of this complex virus in order to dissect the nature of the immune response. Our approach has been to investigate the immune response to individual glycoproteins of HSV-1 by expressing the appropriate genes in mouse L cells. In this system, the glycoproteins are expressed in isolation but are still presented at the cell surface analogous to infected cells. Our reason for choosing glycoproteins is that they are likely to represent major target antigens of the immune system: this is true for the antibody response (for review, see Norrild, 1985) and there is evidence to suggest that glycoproteins are the major targets for both major histocompatibility complex (MHC) class I and class II restricted T lymphocytes (Carter et al., 1981 ;Lawman et al., 1980;Glorioso et al., 1985;Schrier et al., 1983).In this paper we report the establishment of L cells expressing either glycoprotein B (gB) or D (gD) and the use of these lines to study the specificity of the T cell response to HSV-1. The lines were also used to immunize mice against primary virus infections and to prevent the establishment of latent infections.

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“…The glycoproteins are involved in adsorption, entry and cell-to-cell spread of the virus during infection, and can be targets for both humoral and cellular immune responses. Four HSV glycoproteins (gB, gC, gD and gE) have been identified for some time and their genomic map positions and nucleotide sequences determined (Bzik et al, 1984;Pellet et al, 1985;Frink et al, 1983;Watson et al, 1982;McGeoch et al, 1985). However, relatively little is known about their specific biological functions (for review, see Spear, 1984).…”

Section: Introductionmentioning

confidence: 99%

Expression and Characterization of Herpes Simplex Virus Type 1 (HSV-1) Glycoprotein G (gG) by Recombinant Vaccinia Virus: Neutralization of HSV-1 Infectivity with Anti-gG Antibody

Sullivan

Smith

1987

Journal of General Virology

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SUMMARYA recombinant vaccinia virus expressing herpes simplex virus type 1 (HSV-1) glycoprotein G (gG) has been constructed. Cells infected with this recombinant virus (gG-VAC) synthesized glycosylated proteins of 48K, 57K and 61K tool. wt. that were recognized by anti-HSV-1 sera. Rabbits and mice vaccinated with the live recombinant virus produced antibodies that recognized 48K, 57K and 61K mol. wt. proteins in HSV-l-infected cells. The gG polypeptides were present on cytoplasmic and nuclear membranes during infection with both HSV-1 and recombinant vaccinia virus gG-VAC. The 57K and 61K tool. wt. gG polypeptides were present in purified HSV-1 virions and were targets for antibody-mediated complement-dependent virus neutralization.

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Herpes Simplex Virus Type-1 Glycoprotein D Gene: Nucleotide Sequence and Expression in Escherichia coli

Cited by 257 publications

References 23 publications

Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion

Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion

Specificity of the Immune Response of Mice to Herpes Simplex Virus Glycoproteins B and D Constitutively Expressed on L Cell Lines

Expression and Characterization of Herpes Simplex Virus Type 1 (HSV-1) Glycoprotein G (gG) by Recombinant Vaccinia Virus: Neutralization of HSV-1 Infectivity with Anti-gG Antibody

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