Monoclonal antibodies to two glycoproteins of herpes simplex virus type 2

Balachandran, N.; Harnish, Delsworth G.; Killington, R. A.; Bacchetti, Silvia; Rawls, William E.

doi:10.1128/jvi.39.2.438-446.1981

Cited by 58 publications

(44 citation statements)

References 24 publications

(21 reference statements)

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“…Herpes simplex viruses specify a number of glycoproteins (2,3,8,9,21,24) which are located on the virion envelope as well as on the surface of infected cells. These glycoproteins have been termed "social" proteins (14) since they mediate interactions between virions and host cells (24,26,27), between infected cells (11,19), and between various components of the immune system and virions or infected cells (15,23,26,27).…”

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confidence: 99%

Herpesvirus-induced "early" glycoprotein: characterization and possible role in immune cytolysis

Misra¹,

Gilchrist²,

Weinmaster³

et al. 1982

J Virol

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Glycoprotein GVP-11 (molecular weight, 71,500), induced by bovine herpesvirus type 1, was detected on the external surface of infected cells. It could be categorized as an "early" or "beta" class protein since it was synthesized early in the infectious process and its expression was not dependent upon prior viral DNA replication in the infected cells. Monoclonal antibodies directed against GVP-11 immunoprecipitated that glycoprotein and some low-molecular-weight polypeptides from infected cells labeled with either [35S]methionine or [3H]glucosamine. Immunoprecipitation of extracts from cells surface labeled with 125I yielded an additional 138,000-molecular-weight polypeptide. Tunicamycin- or bromovinyl deoxyuridine-treated infected cells yielded polypeptides that were smaller in size than corresponding glycoproteins in untreated cells. Tunicamycin-sensitive glycosylation appeared to be necessary for the expression of the glycoproteins on the surface of the infected cells. The monoclonal antibodies directed against GVP-11 and serum from an immune cow could participate in antibody- and complement-mediated immunocytolysis of infected cells, and this immunocytolysis could be enhanced by arresting cells in the early phase of viral gene expression by treatment with inhibitors of viral DNA synthesis.

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confidence: 99%

Herpesvirus-induced "early" glycoprotein: characterization and possible role in immune cytolysis

Misra¹,

Gilchrist²,

Weinmaster³

et al. 1982

J Virol

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“…The kinetics of appearance of both gC-1 and gC2 in infected cells showed that the proteins could only be clearly detected in cells labeled 3 to 5 h postinfection and not in the presence of DNA synthesis inhibitors, whereas other glycoproteins could be detected as early as 1 to 3 h postinfection (3,26). gC is present on the membrane of HSV-infected cells (3,23,44) as well as on the virion surface (44).…”

mentioning

confidence: 98%

“…In another study with intertypic recombinant viruses (20), an HSV-2 glycoprotein of 63,000 daltons with no apparent HSV-1 counterpart was mapped between 0.55 and 0.65 m.u. Monoclonal antibodies (MABs) to HSV-2 glycoproteins also detected a small glycoprotein with a molecular weight of 60,000 which could be chased into higher-molecular-weight forms of 66,000 and 79,000 (3,4) and was designated gF. Results from two studies with monoclonal antibodies (44,45) showed that HSV-2 gF shared antigenic determinants with HSV-1 gC.…”

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confidence: 99%

“…The newly synthesized and processed forms of gC-2 have been identified. In one report in which Vero cells were infected with HSV-2 strain 333, molecular weights of 60,000 for the precursor and 66,000 and 79,000 for the processed forms were reported (3). In another report, HEp-2 cells were infected with the same strain of virus and the precursor appeared as a doublet of 67,000 and 69,000 which could be chased into a 75,000-molecularweight (75K) mature form (44).…”

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confidence: 99%

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Characterization of the gene encoding herpes simplex virus type 2 glycoprotein C and comparison with the type 1 counterpart

Swain¹,

Peet²,

Galloway³

1985

J Virol

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The gene encoding the glycoprotein C (gC) of herpes simplex virus type 1 maps to the region of the viral genome from 0.62 to 0.64. Recently, a herpes simplex virus type 2 glycoprotein previously designated gF and now designated gC was mapped to a homologous location. Analysis of the herpes simplex virus type 2 mRNA species encoded in this region revealed a major transcript of 2.5 kilobases, a 0.73-kilobase transcript (the 5' ends of which were mapped by primer extension), and several minor species, all nearly identical to the herpes simplex virus type 1 pattern. A polypeptide of ca. 60,000 daltons was identified by in vitro translation of hybrid-selected mRNA. A smaller protein of ca. 20,000 daltons was also mapped to this region. The nucleotide sequence of a 3.4-kilobase segment of DNA encompassing gC was determined, and an open reading frame of 1,440 nucleotides specifying a 480-amino acid protein with properties consistent with that of a glycoprotein was identified. Comparative DNA sequence analysis showed regions of limited homology within the coding sequences for gC and a deletion which results in 31 fewer amino acids in the gC-2 near the amino terminus of the protein. The carboxy termini of gC-1 and gC-2 are very similar, as are the 20,000-dalton proteins. 561 on July 6, 2020 by guest

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“…Monoelonal antibodies to HSV-1 are able to recognize specific individual proteins (3,4) and glycopioteitis (3)(4)(5)(6)(7)(8)(9) as shown by radioitntnuiioptecipitation and polyaerylamide gel eleetrophoresis. Similarly, immunolluorescent staining has been applied to demonstrate the existence of speeific antigens in infected cells and some reports have documented the locations of particular proteins (4,9,10).…”

mentioning

confidence: 99%

Detection of herpes simplex virus proteins in cultured cells by monoclonal antibodies and the avidin‐biotin‐immunoperoxidase complex method

Hwang¹,

Greenspan

Shillitoe³

1986

J Oral Pathology Medicine

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Hwang CBC, Greenspan .IS, Shillitoe E.I. Deteetion of herpes simplex virus proteins in eultuted eells by monoclonal antibodies and the avidin-biotinimmunopeioxidase complex tnefhod. J Oral Pathol 1986: 15: 179-184 Abstract -The distribution of 5 proteins of herpes simplex virus Type 1 was observed in eells that had been infected lor various periods. Tbe cells wete stained with tnonoclonal antibodies to ICP4, 1CP5, ICP6, ICP8, and gB, using the avidin-biotin-peroxidase cotnplex (ABC) method. Eaeh protein had a characteristic pattern of time of appeatanee and translocation by which it could be distinguished from the others. The sensitivity of the ABC technique, its ease of use, and the permanence of the preparations make this method well suited for the study of viral ptoteins.

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Monoclonal antibodies to two glycoproteins of herpes simplex virus type 2

Cited by 58 publications

References 24 publications

Herpesvirus-induced "early" glycoprotein: characterization and possible role in immune cytolysis

Herpesvirus-induced "early" glycoprotein: characterization and possible role in immune cytolysis

Characterization of the gene encoding herpes simplex virus type 2 glycoprotein C and comparison with the type 1 counterpart

Detection of herpes simplex virus proteins in cultured cells by monoclonal antibodies and the avidin‐biotin‐immunoperoxidase complex method

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