Successful Use of Oligopeptides as Immunogens in the Preparation of Antisera to Immediate-Early Gene Products of Herpes Simplex Virus Type 1

Palfreyman, John W.; Maclean, Jean B.; Messeder, Evelyn; Sheppard, R. C.

doi:10.1099/0022-1317-65-5-865

Cited by 10 publications

(2 citation statements)

References 28 publications

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“…The following monoclonal antibodies were used to detect specific HSV proteins: 58S (ICP4) and 19S (gC) (38); 74S (p40) (M. Zweig, personal communication); Ql (alkaline exonuclease) (5); II 481B-2 (gE) (25); 18 m B3 (gD) (3); A4-2 (ICP8), 13 a A5 (ribonucleotide reductase), B2 (gB) and a-E-10 (control) ( M. J. Evelegh and S. Bacchetti, unpublished data). ICP47 was detected after immunoprecipitation with the IE12/76 antiserum (30).…”

Section: Methodsmentioning

confidence: 99%

Cells that constitutively express the herpes simplex virus immediate-early protein ICP4 allow efficient activation of viral delayed-early genes in trans

Persson¹,

Bacchetti²,

Smiley³

1985

J Virol

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To study the role of herpes simplex virus type 1 immediate-early proteins in the transcriptional activation of herpes simplex virus genes, we isolated stably transformed cells expressing herpes simplex virus type 1 ICP4, an immediate-early protein known from previous studies to be necessary for delayed-early and late transcription. These cells efficiently expressed six delayed-early herpes simplex virus genes introduced by viral superinfection, in the absence of de novo viral protein synthesis. In contrast, the delayed-early gene encoding alkaline exonuclease and the late gene encoding the capsid protein VP5 were expressed at much lower levels. Expression of a second late gene, that for glycoprotein C, was undetectable under the same experimental conditions. These results suggest that many, but not all, delayed-early genes are efficiently activated by ICP4; in addition, they demonstrate that although the late gene for VP5 is detectably activated by ICP4, its full expression requires additional factors.

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Section: Methodsmentioning

confidence: 99%

Cells that constitutively express the herpes simplex virus immediate-early protein ICP4 allow efficient activation of viral delayed-early genes in trans

Persson¹,

Bacchetti²,

Smiley³

1985

J Virol

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“…The functions of many viral proteins are not known, e. g. only little is known about the function of ALPHA proteins (1,2,6,30,38). O n the other hand, e.g.…”

Section: Characterization Of Viral Functionsmentioning

confidence: 99%

The Construction, Selection, Characterization, and Application of Recombinant Herpes Viruses

Ackermann¹

1988

Journal of Veterinary Medicine, Series B

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and ConclusionsVarious strategies exist for the construction and selection of recombinant herpes viruses. In order to separate recombinant progeny from the parent viruses, it is necessary to characterize the viruses carefully before and after the recombination events.It is possible to favour the growth of recombinants and to minimize the replication of the parent viruses at the same time by the application of pressure, in most cases using the viral thymidine kinase (TK) as selectable enzyme. In certain instances recombinants may also be picked directly out of a mixed population following nondestructive identification of surface antigens.A large range of applications is open to recombinant herpes viruses. They may be used for mapping genes, their products, and even sequences responsible for the regulation of the gene expression. This knowledge may be applied for the general understanding of the biology of the herpes viruses. A most promising application of recombinant herpes viruses may be their use as vectors for the expression of foreign genes, e. g. in vaccine research. Herpes viruses are able to express foreign genes at high levels. Furthermore, they specify foreign proteins with similar posttranslational modifications as the authentic gene product.

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Characterization of a herpes simplex virus regulatory protein: Aggregation and phosphorylation of a temperature-sensitive variant of ICP 4

Faber

Wilcox

1986

Archives of Virology

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The viral polypeptide ICP 4 (or Vmw 175) is synthesized during the immediate early phase of infection by herpes simplex virus (HSV) and is required during the viral reproductive cycle for efficient transcription of delayed early viral genes. Replication of mutant strains of HSV-1 such as tsLB 2 that encode a temperature-sensitive variant of ICP 4 does not proceed beyond the immediate early phase in cells that are infected and maintained at the nonpermissive temperature (NPT). Under these conditions, the immediate early viral polypeptides accumulate to levels that are 10 to 100 fold greater than normal. We have investigated the use of tsLB 2-infected cells maintained at the NPT as a source for substantial amounts of ICP 4 for further characterization. Extraction of ICP 4 from tsLB 2-infected cells requires 0.5 M NaCl and yields aggregates that contain ICP 4, ICP 6, ICP 27, and lesser amounts of other proteins. These large aggregates cannot be disrupted under nondenaturing conditions and thus are not a suitable source for native ICP 4. We have used this overproduced ICP 4 as an antigen to generate ICP 4-specific antibody and for characterization of the primary structure of ICP 4. Analysis of acid-hydrolysed 32P-labeled ICP 4 revealed that the major phosphorylated residues in ICP 4 are phosphoserine and phosphothreonine.

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Successful Use of Oligopeptides as Immunogens in the Preparation of Antisera to Immediate-Early Gene Products of Herpes Simplex Virus Type 1

Cited by 10 publications

References 28 publications

Cells that constitutively express the herpes simplex virus immediate-early protein ICP4 allow efficient activation of viral delayed-early genes in trans

Cells that constitutively express the herpes simplex virus immediate-early protein ICP4 allow efficient activation of viral delayed-early genes in trans

The Construction, Selection, Characterization, and Application of Recombinant Herpes Viruses

Characterization of a herpes simplex virus regulatory protein: Aggregation and phosphorylation of a temperature-sensitive variant of ICP 4

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