The glycoprotein C gene of herpes simplex virus 1 resident in clonal L cell lines manifests two regulatory domains conferring a dominant B and a subordinate γ2 regulation

Arsenakis, Minas; Campadelli-Fiume, Gabriella; Lombardo, Mariateresa; Roizman, Bernard

doi:10.1016/0042-6822(88)90469-2

Cited by 14 publications

(9 citation statements)

References 27 publications

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“…Monoclonal antibodies against gD (clone H170), gC, and hemagglutinin (HA)-specific polyclonal antiserum described elsewhere were purchased from the Goodwin Institute, Plantation, FL (16,21,22). Polyclonal antibodies against IL-13 were purchased from Santa Cruz Biotechnology.…”

Section: Methodsmentioning

confidence: 99%

Engineered herpes simplex virus 1 is dependent on IL13Rα2 receptor for cell entry and independent of glycoprotein D receptor interaction

Zhou

Debinski

et al. 2002

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

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101

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Section: Methodsmentioning

confidence: 99%

Engineered herpes simplex virus 1 is dependent on IL13Rα2 receptor for cell entry and independent of glycoprotein D receptor interaction

Zhou

Debinski

et al. 2002

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

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101

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“…An additional site mapping downstream from the nucleotide +51 was also found (unpublished work).The significant features of Y2 gene regulation are that (i) expression initiates after the onset of DNA synthesis and continues late in infection; (ii) the requirement for viral DNA synthesis is cis-acting; (iii) 72 genes residing permanently or transiently in cells are induced by infection of the cells, but they are regulated as 83 rather than 72 genes; and (iv) it has been reported that the sequences required for 72 regulation encompass the nucleotides immediately upstream from the transcription initiation site but particularly the TATAA box (15)(16)(17)(18)(19)(20).Our approach to the mapping of cis-acting domains is not to destroy individual putative cis-acting sites in search of loss of function but rather to identify the sequences of the 72 gene that confer upon tk, a 13 gene, the phenotypic properties of the donor gene. We report the results of studies of several recombinants containing chimeric y2-tk genes.…”

mentioning

confidence: 99%

Delineation of regulatory domains of early (beta) and late (gamma 2) genes by construction of chimeric genes expressed in herpes simplex virus 1 genomes.

Mavromara-Nazos

Roizman

1989

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

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The (14). An additional site mapping downstream from the nucleotide +51 was also found (unpublished work).The significant features of Y2 gene regulation are that (i) expression initiates after the onset of DNA synthesis and continues late in infection; (ii) the requirement for viral DNA synthesis is cis-acting; (iii) 72 genes residing permanently or transiently in cells are induced by infection of the cells, but they are regulated as 83 rather than 72 genes; and (iv) it has been reported that the sequences required for 72 regulation encompass the nucleotides immediately upstream from the transcription initiation site but particularly the TATAA box (15)(16)(17)(18)(19)(20).Our approach to the mapping of cis-acting domains is not to destroy individual putative cis-acting sites in search of loss of function but rather to identify the sequences of the 72 gene that confer upon tk, a 13 gene, the phenotypic properties of the donor gene. We report the results of studies of several recombinants containing chimeric y2-tk genes.

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“…HSV-1(F) is the prototype HSV-1 used in this laboratory (4). The propagation of thymidine kinasenegative baby hamster kidney (BHK) cells was described elsewhere (5).…”

mentioning

confidence: 99%

Differentiation of multiple domains in the herpes simplex virus 1 protease encoded by the UL26 gene.

Liu

Roizman

1992

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

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Previous studies have shown that the herpes simplex virus 1 gene U,26 encodes a 635-amino acid protease that cleaves approximately 20 amino acids from the carboxyl terminus of itself and ofa 329-amino acid product ofthe UL,26.5 gene. The results of studies with a variety of protease inhibitors showed that the UL26 protease was inhibited by serine protease inhibitors but not by inhibitors of cysteine protease, aspartic acid protease, or metalloprotease. Mutations resulting in amino acid substitutions, deletions, or insertion of stop codons in the gene or of 20-amino acid stretches into the protease have delineated the dispensable domains I and IV at the amino and carboxyl domains of the gene product. The essential carboxylproximal domain (Ill) can be separated from the essential amino-proximal domain (H) by at least 20 amino acids. The amino-proximal domain is the most conserved region among varicella-zoster virus and human cytomegalovirus homologues of UL26. Of the conserved aspartic acid, histidine, or serine amino acids in this domain, only histidine-61 and -148 could not be replaced without impairment of the proteolytic activity.Earlier we reported that the herpes simplex virus 1 (HSV-1) open reading frame (ORF) UL26 encodes a protease (1). The sequence of UL26 (2) predicts that the protease contains 635 amino acids. The substrate of the protease is the protease itself and a more abundant protein encoded by the ORF UL26.5. The promoter of the UL26.5 ORF is imbedded in the 5' terminal domain of the coding sequences of UL26 ORF. Its coding domain is identical to the coding domain of the terminal 329 amino acids of UL26 ORF, and its product was previously designated as the infected-cell protein no. 35 (ICP35) (1,3). The protease and its more abundant substrate are both cleaved by the protease approximately 20 amino acids from its carboxyl terminus. We report here that (i) the activity of the protease is consistent with that of an enzyme with serine at the active site, a seine protease; (ii) the protease protein contains several domains that are not required for its catalytic activity; and (iii) the active site is near

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The glycoprotein C gene of herpes simplex virus 1 resident in clonal L cell lines manifests two regulatory domains conferring a dominant B and a subordinate γ2 regulation

Cited by 14 publications

References 27 publications

Engineered herpes simplex virus 1 is dependent on IL13Rα2 receptor for cell entry and independent of glycoprotein D receptor interaction

Engineered herpes simplex virus 1 is dependent on IL13Rα2 receptor for cell entry and independent of glycoprotein D receptor interaction

Delineation of regulatory domains of early (beta) and late (gamma 2) genes by construction of chimeric genes expressed in herpes simplex virus 1 genomes.

Differentiation of multiple domains in the herpes simplex virus 1 protease encoded by the UL26 gene.

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