Esh avian sarcoma virus codes for a gag-linked transformation-specific protein with an associated protein kinase activity

Ghysdael, J., Neil, J. C., Wallbank, A. M. and Vogt, P. K. (1981) Esh avian sarcoma virus codes for a gag-linked transformation-specific protein with an associated protein kinase activity. Virology, 111(2), pp. 386-400. (doi:10.1016/0042-6822(81)90342-1)

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Abstract

Esh sarcoma virus, initially isolated from a spontaneous tumor of a chicken, transforms fibroblasts in vitro and induces fibrosarcomas in vivo. It is defective for replication, and infectious viral stocks consist of a mixture of a sarcomagenic virus (ESV) and an a avian leukosis virus of subgroup A (EAV) which serves as helper. Cloned stocks of infectious ESV contain two RNA components of Mr, 3 and 1.5 × 106, respectively, as determined by electrophoresis in sodium dodecyl sulfate-polyacrylamide gels. The component of Mr 1.5 × 106 appears to be the genome of defective ESV, since it is not detected in preparations of the helper virus EAV. The size of the ESV genome suggests major deletions of replicative genes, and ESV-transformed nonproducer cells fail to express functional translation products of the gag, pol, and env genes. ESV-transformed producer and nonproducer clones also do not express pp60src but contain a gag-related protein of Mr 80,000 (p80). Two-dimensional analyses of the [35S]methionine-labeled tryptic peptides of p80 indicate that this protein contains part of the sequences of gag-p19 covalently linked to additional sequences unrelated to gag, pol, and env gene products. These ESV-specific sequences are also unrelated to pp60src and to gag-linked polyproteins found in cells transformed by defective avian sarcoma viruses PRCII and Fujinami or defective leukemia viruses AEV, MC29, and MH2. P80 is phosphorylated in vivo at two major sites, one involving phosphoserine and the other phosphotyrosine residues. Immunoprecipitates containing ESV-p80 are associated with a protein kinase activity that is specific for tyrosine residues of several acceptor molecules including p80 itself, rabbit immunoglobulin H chain of the immune complex and exogenously added α-casein. p80 is phosphorylated in vitro at the same tyrosine site as in vivo suggesting that the enzyme activity detected in vitro is of physiological significance. The p80-associated protein kinase activity is strictly dependent on the presence of Mg2+ or Mn2+ but was found independent of known effectors of cellular protein kinases Ca2+, cAMP, or cGMP.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Neil, Professor James
Authors: Ghysdael, J., Neil, J. C., Wallbank, A. M., and Vogt, P. K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Virology
Publisher:Elsevier
ISSN:0042-6822
ISSN (Online):1096-0341
Published Online:23 February 2004

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