A temperature-sensitive mutant of herpes simplex virus defective in glycoprotein synthesis

Schaffer, Priscilla A.; Courtney, Richard J.; McCombs, Robert M.; Benyésh-Melnick, Matilda

doi:10.1016/0042-6822(71)90037-7

Cited by 33 publications

(15 citation statements)

References 15 publications

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“…TK negative viruses, however, possess the ability to incorporate tritiated thymidine into viral DNA [8], indicating that herpesvirus is able to utilize cell TK. If a functional TK were produced in cells simultaneously infected with TK " mutant pairs, this result might suggest thatTK is composed of different subunits, which polymerize to form the active molecule.…”

Section: Discussionmentioning

confidence: 99%

“…Human embryonic lung (HEL) cells in 16-oz. prescription bottles and tubes were propagated in Eagle's medium supplemented with 10% fetal bovine serum (FBS) and 0.075 % NaHCCU as previously described [8], Cultures were maintained in Eagle's medium containing 5% FBS and 0.15% NaHCC>3 . Cells in Petri dishes were propagated and maintained in Eagle's medium supplemented with 10 and 5 % FBS, respectively, containing 0.225 % NaHCOj in a 5 % CO2 atmosphere.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Thymidine Kinase Activity of Herpes Simplex Virus Temperature-Sensitive Mutants

Aron¹,

Schaffer²,

Courtney³

et al. 1973

Intervirology

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Eighteen temperature-sensitive (ts) mutants of herpes simplex virus type 1 were studied with regard to their ability to synthesize virus-induced thymidine kinase (TK) at permissive (34°) and nonpermissive (39°) temperatures. Five mutants were TK^– at both temperatures (TK^– mutants), 10 were TK⁺ at both temperatures (TK⁺ mutants) and 3 showed reduced TK activity at 39° but not at 34° (TK^± mutants). Two of the 3 TK^± mutants were ts in the production of TK at 39° while the third mutant synthesized a ts TK at both temperatures. Polyacrylamide gel electrophoresis of extracts of both uninfected and TK-mutant-infected cells exhibited one major and one minor peak of TK activity, whereas extracts of wild-type (WT) virus-infected cells revealed at least one additional major peak of TK activity. Gel patterns of TK^± mutants were similar to those of the WT virus in 34 and 39° extracts; however, a reduction in TK activity of the viral peaks was observed in 39° extracts.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Thymidine Kinase Activity of Herpes Simplex Virus Temperature-Sensitive Mutants

Aron¹,

Schaffer²,

Courtney³

et al. 1973

Intervirology

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“…permissive temperature (6,7,21,24). Intrinsic labeling experiments with [35S]methionine were undertaken to characterize the viral polypeptides synthesized under nonpermissive conditions by group E, ts-8, and ts-18 mutant infections.…”

Section: Immune Lysis Of Mutant Hsv-infected Cells 677mentioning

confidence: 99%

Mutant analysis of herpes simplex virus-induced cell surface antigens: resistance to complement-mediated immune cytolysis

Glorioso¹,

Levine²,

Holland³

et al. 1980

J Virol

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BHK-21 cells infected with temperature-sensitive mutants of herpes simplex virus type 1 strain KOS representing 16 complementation groups were tested for susceptibility to complement-mediated immune cytolysis at permissive (34 degrees C) and nonpermissive (39 degrees C) temperatures. Only cells infected by mutants in complementation group E were resistant to immune cytolysis in a temperature-sensitive manner compared with wild-type infections. The expression of group E mutant cell surface antigens during infections at 34 and 39 degrees C was characterized by a combination of cell surface radioiodination, specific immunoprecipitation, and gel electrophoretic analysis of immunoprecipitates. Resistance to immune lysis at 39 degrees C correlated with the absence of viral antigens exposed at the cell surface. Intrinsic radiolabeling of group E mutant infections with [14C]glucosamine revealed that normal glycoproteins were produced at 34 degrees C but none were synthesized at 39 degrees C. The effect of 2-deoxy-D-glucose on glycosylation of group E mutants at 39 degrees C suggested that the viral glycoprotein precursors were not synthesized. The complementation group E mutants failed to complement herpes simplex virus type 1 mutants isolated by other workers. These included the group B mutants of strain KOS, the temperature-sensitive group D mutants of strain 17, and the LB2 mutant of strain HFEM. These mutants should be considered members of herpes simplex virus type 1 complementation group 1.2, in keeping with the new herpes simplex virus type 1 nomenclature.

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“…It is likely, however, that sequences outside of these relatively small fragments have been transferred in addition, although further work is necessary to determine this. HSV-1 strains KOS, McKrae, d/Pstflgal and MK13 were tested in one-step growth assays in Vero cells as previously described (Schaffer et al, 1971) and each of the viruses grew to high titres with comparable kinetics (data not shown). We next tested the abilities of these viruses to replicate and reactivate in vivo.…”

confidence: 99%