Isolation of a Tumour Virus from a Chicken submitted to a Poultry Diagnostic Laboratory–Esh Sarcoma Virus

Wallbank, Alfred M.; Sperling, F. George; Hubben, K; Stubbs, E. L.

doi:10.1038/2091265a0

Cited by 16 publications

(4 citation statements)

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“…Yamaguchi 73 sarcoma virus (Y73) and Esh sarcoma virus (ESV) are replication-defective transforming retroviruses that were independently isolated from spontaneous sarcomas in chickens (25,46). Both viruses induce sarcomas in vivo and are able to transform fibroblastic cells in vitro (19,26).…”

mentioning

confidence: 99%

Common features of the yes and src gene products defined by peptide-specific antibodies

Gentry¹,

Rohrschneider²

1984

J Virol

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Anti-peptide antibodies generated against a hydrophilic domain of pp6Osrc comprising amino acid residues 498 through 512 were shown to be cross-reactive with the corresponding region in the yes transforming proteins encoded by Yamaguchi 73 and Esh sarcoma viruses. This cross-reactivity was demonstrated by immunoblot and immunoprecipitation analyses, and the identity of the proteins was verified by partial proteolytic mapping. By utilizing a combination of immunofluorescence and interference-reflection microscopy, these cross-reactive anti-peptide antibodies were shown to produce an immunofluorescence staining pattern in Yamaguchi 73 and Esh sarcoma virus-transformed chicken embryo fibroblasts remarkably similar to that of pp60src in Rous sarcoma virus-infected chicken cells. Like the src gene products, the yes transformation-specific polyproteins were found to be concentrated within adhesion plaque structures and needle-like interdigitating cell-cell junctions. This analogous subcellular distribution suggests that these onc proteins are functionally related and may share common intracellular targets.

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confidence: 99%

Common features of the yes and src gene products defined by peptide-specific antibodies

Gentry¹,

Rohrschneider²

1984

J Virol

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“…Expression of the 59-and 62-kilodalton proteins, determined by the immune complex kinase assay, was relatively high in brain, retina, kidney, and liver. The presence in normal chicken embryo fibroblasts and in chicken kidney of two transcripts, 3.7 and 3.9 kilobases in length, that hybridize with a yes-specific DNA probe, as well as the two proteins recognized by anti-yes IgG, suggests either differential splicing of cellular yes gene transcripts or the existence of another yes-related gene.Yamaguchi 73 (Y73) and Esh avian sarcoma viruses are replication-defective retroviruses that were independently isolated from spontaneous tumors in chickens (16,42). Both viruses induce sarcomas in vivo and transform chicken embryo fibroblasts (CEF) in vitro (11, 18).…”

mentioning

confidence: 99%

“…Yamaguchi 73 (Y73) and Esh avian sarcoma viruses are replication-defective retroviruses that were independently isolated from spontaneous tumors in chickens (16,42). Both viruses induce sarcomas in vivo and transform chicken embryo fibroblasts (CEF) in vitro (11,18).…”

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confidence: 99%

Cellular proteins homologous to the viral yes gene product.

Sudol¹,

Hanafusa²

1986

Mol. Cell. Biol.

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We raised antibodies in rabbits against the amino-terminal portion of the viral yes protein produced in bacteria with the use of an expression vector based on the lac operon. The anti-yes serum thus obtained precipitated p9Wgag-yes from Yamaguchi 73 virus-transformed chicken embryo fibroblasts, and this immunoprecipitation was blocked by the purified antigen. The anti-yes serum did not recognize viral src, fps, or fgr proteins. Affinity-purified anti-yes immunoglobulin G (IgG) precipitated two proteins of 59 and 62 kilodaltons from lysates of normal chicken embryo fibroblasts. Two-dimensional tryptic peptide mapping showed that these proteins are closely related to p9A09-yes and that they are different from pp60c-S. Similar to P90919-y", the 59-and 62-kilodalton proteins were phosphorylated exclusively on tyrosine in an in vitro kinase reaction, whereas in vivo they were phosphorylated on serine and, to a lesser extent, on tyrosine as well. Expression of the 59-and 62-kilodalton proteins, determined by the immune complex kinase assay, was relatively high in brain, retina, kidney, and liver. The presence in normal chicken embryo fibroblasts and in chicken kidney of two transcripts, 3.7 and 3.9 kilobases in length, that hybridize with a yes-specific DNA probe, as well as the two proteins recognized by anti-yes IgG, suggests either differential splicing of cellular yes gene transcripts or the existence of another yes-related gene.Yamaguchi 73 (Y73) and Esh avian sarcoma viruses are replication-defective retroviruses that were independently isolated from spontaneous tumors in chickens (16,42). Both viruses induce sarcomas in vivo and transform chicken embryo fibroblasts (CEF) in vitro (11, 18). The transforming properties of these viruses are directed by cell-derived sequences called yes (33,43). The yes transforming genes of Y73 and Esh avian sarcoma virus encode pg9yag-yes and P80Iag-Yes phosphoproteins, respectively (10, 18). The amino acid sequence of the p90yag-yes fusion protein predicted from the DNA sequence of the Y73 genome (19) shows a high degree of homology with pp60v-rc, the transforming protein of Rous sarcoma virus (31, 40). The greatest extent of homology exists in the carboxy-terminal domains, whereas the amino-terminal portions of these two oncogene proteins are different (19).Our interest in cellular yes (c-yes) proteins(s) stems from two initial observations. Studies at the RNA level have shown that c-yes expression in various chicken tissues is one to two orders of magnitude higher than that of other known c-onc sequences from the avian sarcoma virus family, and that the pattern of tissue-specific expression of c-yes shows elevated levels of c-yes mRNA in kidney and brain (33).In this report, we describe the characterization of two cellular proteins of 59 and 62 kilodaltons (kDa) immunoprecipitated from normal chicken cells with antibodies raised against the amino-terminal portion of the viral yes (v-yes) protein expressed in bacteria. By a number of criteria we show that these proteins are clo...

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“…The Yes kinase was originally discovered as the oncogenic protein encoded by the Yamaguchi 73 and Esh sarcoma viruses (2)(3)(4)(5)(6). Initial interest in v-Yes arose as a result of its similarity to v-Src.…”

Section: V-yes and V-srcmentioning

confidence: 99%

Specificity in signaling by c-Yes

Flynn¹

2003

Front Biosci

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c-Yes and c-Src are the two most closely related members of the Src family of nonreceptor tyrosine kinases. Although there is much evidence to support redundancy in signaling between these two kinases, there is also a growing body of evidence to indicate specificity in signaling. In this review, we summarize c-Yes, its potential functions and its ability to modulate signals that are distinct from c-Src.

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Isolation of a Tumour Virus from a Chicken submitted to a Poultry Diagnostic Laboratory–Esh Sarcoma Virus

Cited by 16 publications

References 1 publication

Common features of the yes and src gene products defined by peptide-specific antibodies

Common features of the yes and src gene products defined by peptide-specific antibodies

Cellular proteins homologous to the viral yes gene product.

Specificity in signaling by c-Yes

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