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. 1989 Mar;33(3):400–403. doi: 10.1128/aac.33.3.400

Characterization of a halothane-resistant strain of measles virus.

E Bedows 1, B A Davidson 1, B A Williams 1, P R Knight 1
PMCID: PMC171503  PMID: 2658788

Abstract

A strain of measles virus (MVr) whose replication demonstrated increased resistance to halothane (2-bromo-2-chloro-1,1,1-trifluoroethane) exposure compared with the susceptible parental strain (MVs) is described. After exposure to a 1.2% halothane concentration, substantial amounts of the measles virus H protein were detected in MVr-infected Vero cell lysates by immunoprecipitation and polyacrylamide gel electrophoresis or by quantitative immunofluorescence staining. The protein was barely detectable in identically treated MVs-infected lysates, however. The recovery of all other measles virus proteins studied was the same in MVr- and MVs-infected cells at this anesthetic concentration. Thus, the altered expression of a single gene product appears to be responsible for the observed halothane resistance.

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Selected References

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  1. Aune H., Bessesen A., Olsen H., Mørland J. Acute effects of halothane and enflurane on drug metabolism and protein synthesis in isolated rat hepatocytes. Acta Pharmacol Toxicol (Copenh) 1983 Nov;53(5):363–368. doi: 10.1111/j.1600-0773.1983.tb03436.x. [DOI] [PubMed] [Google Scholar]
  2. Bedows E., Davidson B. A., Knight P. R. Effect of halothane on the replication of animal viruses. Antimicrob Agents Chemother. 1984 Jun;25(6):719–724. doi: 10.1128/aac.25.6.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Haspel M. V., Knight P. R., Duff R. G., Rapp F. Activation of a latent measles virus infection in hamster cells. J Virol. 1973 Oct;12(4):690–695. doi: 10.1128/jvi.12.4.690-695.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Jackson S. H. The metabolic effects of halothane on mammalian hepatoma cells in vitro. II. Inhibition of DNA synthesis. Anesthesiology. 1973 Oct;39(4):405–409. doi: 10.1097/00000542-197310000-00013. [DOI] [PubMed] [Google Scholar]
  5. Johnson G. D., Davidson R. S., McNamee K. C., Russell G., Goodwin D., Holborow E. J. Fading of immunofluorescence during microscopy: a study of the phenomenon and its remedy. J Immunol Methods. 1982 Dec 17;55(2):231–242. doi: 10.1016/0022-1759(82)90035-7. [DOI] [PubMed] [Google Scholar]
  6. Knight P. R., Nahrwold M. L., Bedows E. Anesthetic action and virus replication: inhibition of measles virus replication in cells exposed to halothane. Antimicrob Agents Chemother. 1980 May;17(5):890–896. doi: 10.1128/aac.17.5.890. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  8. Nahrwold M. L., Cohen P. J. Anesthetics and mitochondrial respiration. Clin Anesth. 1975;11(1):25–44. [PubMed] [Google Scholar]
  9. Rannels D. E., Christopherson R., Watkins C. A. Reversible inhibition of protein synthesis in lung by halothane. Biochem J. 1983 Feb 15;210(2):379–387. doi: 10.1042/bj2100379. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Tait A. R., Knight P. R. The effects of general anesthesia on upper respiratory tract infections in children. Anesthesiology. 1987 Dec;67(6):930–935. doi: 10.1097/00000542-198712000-00009. [DOI] [PubMed] [Google Scholar]
  11. Welsh M. J. Localization of calmodulin and calmodulin acceptor sites by fluorescence methods. Methods Enzymol. 1983;102:110–121. doi: 10.1016/s0076-6879(83)02012-1. [DOI] [PubMed] [Google Scholar]

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