Restricted replication of vesicular stomatitis virus in T lymphocytes is coincident with a deficiency in a cellular protein kinase required for viral transcription

• Published in: Journal of general virology Vol. 73; no. 12; pp. 3125 - 3132
• Main Authors: Sleat, David E, Chikkala, Nathaniel F, Gautam, Subhash, Banerjee, Amiya K
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01-12-1992; Society for General Microbiology
• Subjects: Animals; Biological and medical sciences; Casein Kinases; Cells, Cultured; Cercopithecus aethiops; Cricetinae; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Viral; Humans; In Vitro Techniques; Microbiology; Phosphoproteins - metabolism; Phosphorylation; Protein Kinases - deficiency; Protein Kinases - metabolism; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; T-Lymphocyte Subsets - microbiology; Transcription, Genetic; Vesicular stomatitis Indiana virus - growth & development; Vesiculovirus; Viral Nonstructural Proteins - metabolism; Virology; Virus Replication; Virus multiplication; Transcription; Enzyme; Host; Host virus relation; Virus; Infection; Vesicular stomatitis virus; Vesiculovirus; Rhabdoviridae; Protein kinase; T-Lymphocyte; Replication; Defectivity
• DOI: 10.1099/0022-1317-73-12-3125
• EISSN: 1465-2099
• ISSN: 0022-1317

1 Department of Molecular Biology
and 2 Section of Immunology, Department of General Medical Sciences, Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, U.S.A.
Vesicular stomatitis virus (VSV) fails to replicate in mouse T lymphocytes unless the cells have been mitogenically stimulated with concanavalin A (Con A). We have examined the possibility that the failure of VSV to replicate in unstimulated T lymphocytes can be attributed to a deficiency in a host protein kinase which activates the viral P protein by phosphorylation, thus rendering it transcriptionally competent. Soluble extracts were prepared from purified mouse T lymphocytes, with or without prior treatment with Con A. The ability of these extracts to phosphorylate bacterially synthesized P protein of two VSV serotypes was measured in vitro . Activity of the protein kinase on the P proteins of the Indiana or New Jersey serotypes of VSV increased, on average 2.4- and 2.1-fold respectively, after treatment of the cells with 3 µg/ml Con A. Higher concentrations of Con A induced proportional increases (up to 10-fold) in the activity of the host protein kinase. Activities of the kinase phosphorylating the P protein in separate populations of CD4- and CD8-containing murine T lymphocytes increased similarly on mitogenic activation. No biochemical or immunological differences were observed between the T cell protein kinase and the previously characterized protein kinase (casein kinase II) from BHK-21 cells. The activity of the kinase that phosphorylates the P protein did not vary in CV-1 cells on treatment with - or -interferon, both of which inhibited VSV replication. Similarly, casein kinase II activities in Raji and SIRC cells, which do not normally support VSV growth, were the same as in BHK-21 cells. Thus restriction of VSV replication in these cells, in contrast to T lymphocytes, was not associated with a deficiency in the host casein kinase II activity.
Present address: Division of Medical Oncology/Hematology, Henry Ford Hospital, Detroit, Michigan 48202-2689, U.S.A.
Received 28 May 1992;
accepted 4 September 1992.