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PubMed1982

[The effect of sodium nitrite on rats infected with avian sarcoma virus].

A potential effect of sodium nitrite was studied as exerted on carcinogenesis elicited by the avian sarcoma virus in the body of rats. In the case of the infection of the rats with indefective avian sarcoma virus B77 (Bratislava strain; ID50 10-25/0.1 ml) and i. p. inoculation of sodium nitrite, great mortality occurred already on the 20th day p. i. On the 125th day p. i. the cumulative mortality in this group was 76.92%; on the other hand, in the control groups (rats inoculated with sodium nitrite or avian sarcoma virus) no deaths occurred before this period. The rats infected with a double dose of the virus were not observed to show pronounced changes in mortality. It was only on the 125th day that cumulative mortality in the group of rats infected with the avian sarcoma virus and rats inoculated s. c. with sodium nitrite was 87.5% and in the group of animals which had only been infected with the virus the mortality was 64.26%. The patho-morphological changes were in keeping with the hitherto described changes in rats infected with the avian sarcoma virus. In the trial no effect of sodium nitrite on the patho-morphological changes induced by the avian sarcoma virus was observed.

Animals↗
PubMed1980

Arrangement of integrated avian sarcoma virus DNA sequences within the cellular genomes of transformed and revertant mammalian cells.

We have examined the arrangement of integrated avian sarcoma virus (ASV) DNA sequences in several different avian sarcoma virus transformed mammalian cell lines, in independently isolated clones of avian sarcoma virus transformed rat liver cells, and in morphologically normal revertants of avian sarcoma virus transformed rat embryo cells. By using restriction endonuclease digestion, agarose gel electrophoresis, Southern blotting, and hybridization with labeled avian sarcoma virus complementary DNA probes, we have compared the restriction enzyme cleavage maps of integrated viral DNA and adjacent cellular DNA sequences in four different mouse and rat cell lines transformed with either Bratislava 77 or Schmidt-Ruppin strains of avian sarcoma virus. The results of these experiments indicated that the integrated viral DNA resided at a different site within the host cell genome in each transformed cell line. A similar analysis of several independently derived clones of Schmidt-Ruppin transformed rat liver cells also revealed that each clone contained a unique cellular site for the integration of proviral DNA. Examination of several morphologically normal revertants and spontaneous retransformants of Schmidt-Ruppin transformed rat embryo cells revealed that the internal arrangement and cellular integration site of viral DNA sequences was identical with that of the transformed parent cell line. The loss of the transformed phenotype in these revertant cell lines, therefore, does not appear to be the result of rearrangement or deletions either within the viral genome or in adjacent cellular DNA sequences. The data presented support a model for ASV proviral DNA integration in which recombination can occur at multiple sites within the mammalian cell genome. The integration and maintenance of at least one complete copy of the viral genome appear to be required for continuous expression of the transformed phenotype in mammalian cells.

Animals↗
PubMed1987

Effect of phorbol myristate acetate on cultured tumor cells derived from different stages of avian sarcoma virus (ASV)-induced neoplastic growth.

We have investigated the action of the tumor promoter phorbol 12-myristate-13-acetate (PMA) on avian sarcoma cells cultured from avian sarcoma virus (ASV)-induced tumors at various stages of growth and on normal chicken embryo fibroblasts (CEF). We found that exposure to PMA (30 ng/ml) led to decreased expression of the malignant phenotype of avian sarcoma cells which had been derived from progressively-growing or regressing neoplasms. For example, treatment with PMA caused inhibition of growth of cultured avian tumor cells as well as decreased synthesis of DNA and protein. In addition, such treatment resulted in reduced expression of pp60src kinase activity. Direct inoculation of PMA into growing avian sarcomas led to an enhancement of the tumor regression which occurs in this system as a consequence of a strong cell-mediated, anti-tumor immune response.

Animals↗
PubMed1979

Cellular information in the genome of recovered avian sarcoma virus directs the synthesis of transforming protein.

Recovered avian sarcoma viruses, whose sarcomagenic information is largely derived from cellular sequences [Wang, L.-H., Halpern, C.C., Nadel, M. & Hanafusa, H. (1978) Proc. Natl. Acad. Sci. USA 75, 5812-5816], produce the transforming protein p60src in infected cells, in amounts comparable to the amount found in cells transformed by standard strains of avian sarcoma virus. Though displaying some virus-specific differences in electrophoretic mobility, p60srcs from these viruses are similar to those of other avian sarcoma virus strains by the criteria of (i) antigenicity, (ii) partial proteolysis mapping, and (iii) association with protein kinase activity. We also find that p60sarc, a protein present in normal cells at a low level, is associated with a protein kinase activity, and thus it too is similar by the above criteria to p60src of avian sarcoma virus. Possible causes for the pathogenicity of p60src are discussed in light of these similarities.

Alpharetrovirus↗
PubMed1987

Correlation of neuropathologic findings, computerized tomographic and high-resolution ultrasound scans of canine avian sarcoma virus-induced brain tumors.

The location, size, geometry and neuropathological findings of anaplastic astrocytomas (AA), gliosarcomas and sarcomas induced by the avian sarcoma virus (ASV) in dogs were compared with images generated using computerized tomography (CT) and real time high-resolution ultrasound (HRUS). Seven AA showed a wide range of findings on CT. Pre-contrast CT scans showed that the tumors could be hyper, hypo, or isodense. Three of seven AA had no contrast enhancement; two of these tumors were also isodense which resulted in a false-negative CT exam. Partial enhancement was seen in one tumor. This resulted in a sensitivity of detection of 72%. Real time HRUS was able to define tumor location, size and geometry of the AA missed or incompletely imaged by CT. All tumors were hyperechoic. Inhomogeneity of the echo pattern was due to hemorrhage, cyst formation, and necrosis within the tumors. Such secondary tumor characteristics were more accurately defined by HRUS compared to CT. Vasogenic edema in the brain surrounding tumors was of low density on CT and hypoechoic or indistinguishable from normal brain on US. Similar findings were seen in six gliosarcomas, two of which were not visualized by either pre- or post-contrast enhanced CT scans (sensitivity of 66%). Sarcomas differed in that they were either hyper or isodense; none were hypodense. The area of increased density matched the tumor geometry and correlated with dense cellularity and reticulin deposition. All 13 sarcomas showed contrast enhancement (100% sensitivity), but in two tumors, contrast enhanced CT underestimated the size of the tumor. Because of the large size and multiplicity of the sarcomas, HRUS imaging was not able to resolve the entire tumor volume because of limited imaging access. Intravenously injected horseradish peroxidase (HRP) crossed the tumor blood-brain barrier (BBB) only in those tumors in which contrast enhancement was seen. These studies suggest that intraoperative HRUS imaging may be useful in detecting and delineating human AA incompletely visualized by CT.

Animals↗
PubMed1977

Nucleotide sequence at the 5' terminus of the avian sarcoma virus genome.

Transcription of DNA from the RNA genome of avian sarcoma virus by RNA-directed DNA polymerase in vitro initiates on a primer (tRNATrp) located near the 5'-terminus of the viral genome. One of the major products of transcription is a single-stranded DNA chain complementary to a sequence of 101 nucleotides immediately distal to the site of initiation of DNA synthesis. We have determined the complete nucleotide sequence of this transcribed chain for the Prague strain of avian sarcoma virus, a partial sequence of the transcribed chain for the Bratislava 77 strain of avian sarcoma virus, and the sequence of a DNA transcript that is shorter than the transcribed single-stranded chain. Our data define the location of tRNATrp on the genome of avian sarcoma virus and provide the sequence of 119 nucleotides at the 5'-terminus of the genome. Portions of this sequence may be involved in the binding of RNA-directed DNA polymerase, the initiation of translation from viral messenger RNA, the extension of RNA-directed DNA synthesis from the 5'- to the 3'-terminus of viral RNA, and the integration of viral DNA into the host genome.

Avian Sarcoma Viruses↗
PubMed1984

Fine-structure analyses of lipid-protein and protein-protein interactions of gag protein p19 of the avian sarcoma and leukemia viruses by cyanogen bromide mapping.

In avian sarcoma and leukemia viruses, the gag protein p19 functions structurally as a matrix protein, connecting internal components with the viral envelope. We have used a combination of in situ cross-linking and peptide mapping to localize within p19 the regions responsible for two major interactions in this complex, p19 with lipid and p19 with p19. Lipid-protein cross-links were localized near the amino terminus within the first 35 amino acids of the polypeptide. Homotypic protein-protein disulfide bridges were found to originate from near the carboxy terminus of p19, from cysteine residues at amino acids 111 and 153. These results suggest that p19 is divided into domains with distinct functions. The peptide maps constructed for p19, and for the related proteins p23 in avian sarcoma and leukemia viruses and p19 beta in recombinant avian sarcoma viruses, should serve as useful tools for other types of studies involving these proteins.

Amino Acids↗
PubMed1977

Purification of DNA complementary to the env gene of avian sarcoma virus and analysis of relationships among the env genes of avian leukosis-sarcoma viruses.

The env gene of avian leukosis-sarcoma viruses encodes a glycoprotein that determines the host range and surface antigenicitiy of virions. We have purified radioactive DNA (cDNAgp) complementary to at least a portion of the env gene for viral subgroups A and C; complementary DNA was synthesized with purified virions of wild-type avian sarcoma virus, and RNA from a mutant with a deletion in env was used to select DNA specific to env by molecular hybridization. The genetic complexity of cDNAgp for subgroup A (ca. 2,000 nucleotides) was sufficient to represent the entire deletion and most or all of the env cistron. The deletions in env in two independently isolated strains of virus (Bryan and rdNY8SR) overlap, and cDNAgp represents nucleotide sequences common to both deletions. By contrast, we could detect no overlap between deletions in env and deletions in the adjacent viral gene src. Laboratory stocks of viral subgroups A, B, C, D and E do not contain detectable amounts of env deletions when tested by molecular hybridization; hence, segregation of deletions in env is a less frequent event that the segregation of deletions in the viral transforming gene src (Vogt, 1971). We found extensive homology among the nucleotide sequences encoding the env genes of virus strains indigenous to chickens (subgroups A, B, C, D, and E) although subgorups B, D and E appear to differ slightly from subgroups A and C at the env locus. By contrast, viruses obtained from pheasant cells (subgroups F and G) have env genes with little or no relationship to env genes of chikcen viruses. According to available data, viruses of subgroup F arose by recombination between an avarian sarcoma virus and viral genes in the genome of ring-necked pheasants, whereas subgroup G viruses may be entirely endogenous to golden pheasants.

Alpharetrovirus↗
PubMed1984

Sarcoma growth in 15I5 x 7(2) chickens infected with avian sarcoma viruses of subgroup B or G.

A comparative study was made of sarcoma growth in 15I5 x 7(2) chickens infected in the wing web at 4 weeks of age with strains of subgroup B or G avian sarcoma viruses. Infection with sarcoma viruses of either subgroup B or G resulted in the formation of progressive wing web sarcomas at the site of inoculation. The survival times of the subgroup G virus-infected chickens were generally at least twice as great as the survival times of the subgroup B virus-infected chickens, which averaged 6-9 weeks postinoculation. At 5 weeks postinfection, a significantly higher titer of virus neutralizing antibody was detected in the subgroup G virus-infected chickens. Necropsy indicated that a high percentage of subgroup B virus-infected chickens exhibited fibrosarcomas at sites distal to the primary wing web sarcomas, whereas only a small percentage of subgroup G virus-infected chickens exhibited distal sarcomas. The results further indicated that the viral env gene is a determinant of the pattern of distal sarcoma formation.

Animals↗
PubMed1984

[Characterization of a transforming growth factor produced in rat cells transformed by an avian sarcoma virus].

Transformation of rat cells by avian sarcoma viruses (ASVs) induced the release of transforming growth factors (TGFs), which transiently promote anchorage-dependent untransformed BALB3T3 clone A31 cells to form progressively growing colonies in soft agar, into serum-free conditioned medium. A new class of TGF, which is a heat and acid-labile protein with a molecular mass of 12,000 daltons, was isolated and purified from an ASV-transformed rat cell line, 77N1, derived from NRK cells. The TGF from 77N1 did not bind to epidermal growth factor membrane receptors. We observed specific in vitro phosphorylation of several membrane proteins from A31 cells in the presence of the TGF.

Animals↗
PubMed1995

Differential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses.

The CA (capsid) protein of avian sarcoma and leukemia viruses occurs in multiple species. Only one form has been previously characterized biochemically. We have now determined that the mature CA protein of avian sarcoma and leukemia viruses exists as three species with different C termini, ending in amino acid residues A-476, A-478, and M-479 of the Gag precursor, respectively. These structures were deduced from a combination of cyanogen bromide peptide mapping, sequence analysis of tryptic peptides, and electrospray mass spectrometry. The three forms of CA were detected in the same ratios in Rous sarcoma virus and avian myeloblastosis virus and therefore are likely to represent a common feature of members of this genus of avian retroviruses. The only previously reported CA species, CAM-479, accounts for only about 36% of the total CA protein, while CAA-476 and CAA-478 account for 55 and 9%, respectively. From the analysis of peptides cleaved in vitro by PR, the viral protease, we infer that the cleavage site between A-476 and A-477 not only is recognized by PR but is the preferred site. We were unable to determine if A-478/A-479 is a cleavage site for PR or alternatively if CAA-478 results from further processing of CAM-479 by a carboxypeptidase. To study the biological significance of residues A-477 to M-479, we constructed genetically altered viruses in which deletions removed either residues 477 to 479 or 477 to 488. The resulting virus particles appeared to assembly with normal efficiencies, but the latter mutant showed slowed proteolytic processing. Neither of the mutants was infectious.

Amino Acid Sequence↗
PubMed1982

Avian sarcoma virus UR2 encodes a transforming protein which is associated with a unique protein kinase activity.

UR2 is a newly characterized avian sarcoma virus whose genome contains a unique sequence that is not related to the sequences of other avian sarcoma virus transforming genes thus far identified. This unique sequence, termed ros, is fused to part of the viral gag gene. The product of the fused gag-ros gene of UR2 is a protein of 68,000 daltons (P68) immunoprecipitable by antiserum against viral gag proteins. In vitro translation of viral RNA and in vivo pulse-chase experiments showed that P68 is not synthesized as a large precursor and that it is the only protein product encoded in the UR2 genome, suggesting that it is involved in cell transformation by UR2. In vivo, P68 was phosphorylated at both serine and tyrosine residues. Immunoprecipitates of P68 with anti-gag antisera had a cyclic nucleotide-independent protein kinase activity that phosphorylated P68, rabbit immunoglobulin G in the immune complex, and alpha-casein. The phosphorylation by P68 was specific to tyrosine of the substrate proteins. P68 was phosphorylated in vitro at only one tyrosine site, and the tryptic phosphopeptide of in vitro-labeled P68 was different from those of Fujinami sarcoma virus P140 and avian sarcoma virus Y73-P90. A comparison of the protein kinases encoded by UR2, Rous sarcoma virus, Fujinami sarcoma virus, and avian sarcoma virus Y73 revealed that UR2-P68 protein kinase is distinct from the protein kinases encoded by those viruses by several criteria. Our results suggest that several different protein kinases encoded by viral transforming genes have the same functional specificity and cause essentially the same cellular alterations.

Alpharetrovirus↗
PubMed1982

Cellular sequences related to three new onc genes of avian sarcoma virus (fps, yes, and ros) and their expression in normal and transformed cells.

Two onc genes of avian sarcoma viruses unrelated to the src gene have recently been identified: fps of Fujinami sarcoma virus/PRCII/UR1 and yes of Y73/Esh sarcoma virus. In the first part of this study we demonstrated that UR2, the most recently isolated avian sarcoma virus, contains in its genome a unique sequence, ros, nonhomologous to src, fps, and yes sequences or to transforming genes of avian acute leukemia viruses. Using cDNAs specific to the inserts of avian sarcoma virus genomes, we examined the existence and the transcription of cellular nucleotide sequences related to the three new onc genes of avian sarcoma virus (fps, yes and ros) in various cells. The progenitor cellular sequences for these onc genes (c-onc) were present in uninfected chicken DNA in one or few copies per haploid genome. These c-onc sequences were detectable in cellular DNA of a wide variety of vertebrates, and the homology between viral and cellular onc was inversely related to the phylogenetic distance of animal species. The pattern of expression of these c-onc genes in different tissues of chickens was found to be unique to each gene. The expression of c-fps and c-ros genes was generally repressed in many tissues, but c-fps was expressed at higher levels in bone marrow (2.5 copies per cell) and lung (1.1 copies per cell), whereas c-ros was mainly transcribed in kidney (2.5 copies per cell). On the other hand, c-yes transcripts were easily detectable in all tissues analyzed and were found at high levels in kidney (26 copies per cell). These c-onc expressions were unaffected by infection with avian sarcoma viruses that contained other onc genes. In a few cultures of chicken and quail transformed cells derived from tumors induced by chemical carcinogens, we found that the levels of transcription of the four c-onc genes remained unaltered, compared with that in normal tissues.

Alpharetrovirus↗
PubMed1981

Viral and cellular src genes contribute to the structure of recovered avian sarcoma virus transforming protein.

Recovered avian sarcoma viruses (rASVs) were obtained from tumors induced by certain transformation-defective (td) mutants of Schmidt-Ruppin strain Rous sarcoma virus of subgroup A (SR-A). The genomes of these td SR-A mutants lack most but not all of the src gene. rASV genomes, however, possess intact src genes, which are largely derived from cellular genetic information, presumably an endogenous cellular gene called c-src, which shares considerable homology with the viral src. To further define the genetic origin of rASV src, we examined by tryptic peptide analysis the product of this gene, pp60src, from rASV and SR-A, as well as the normal cellular homolog pp60c-src. We found peptides unique to each putative "parental" protein present together in maps of rASV p60src, demonstrating that the endogenous cellular c-src gene itself contributes to the structure of rASV pp60src. Certain isolates of rASV encode pp60srcS of altered apparent molecular weight. In these cases, the variation in structure was located in the amino-terminal portion of the protein. That such polymorphism can be tolerated suggests that this region of the protein is less critical to the ability of these agents to transform cells.

Amino Acids↗
PubMed1981

A third class of avian sarcoma viruses, defined by related transformation-specific proteins of Yamaguchi 73 and Esh sarcoma viruses.

The gag-linked transformation-specific protein (polyprotein) p80 of Esh avian sarcoma virus (ESV) has been compared by tryptic peptide mapping with the homologous protein p90 of Yamaguchi 73 avian sarcoma virus (Y73). p80 of ESV and p90 of Y73 were found to share all four of their major nonstructural, transformation-specific, methionine-containing peptides and to have at least seven cysteine-containing transformation-specific peptides in common. Two nonstructural cysteine-containing peptides unique for ESV p80 and three specific for Y73 p90 were also identified. None of these peptides were found in the transforming gene product pp60src of Rous sarcoma virus (RSV) or in the transformation-specific polyproteins p105 of avian sarcoma virus PRCII (PRCII) or p140 of Fujinami sarcoma virus (FSV). ESV p80 and Y73 p90 are phosphorylated, and their tryptic phosphopeptides appear to be identical. In each polyprotein two major phosphopeptides were demonstrated, one containing phosphoserine, the other phosphotyrosine. The latter serves as phosphoacceptor for the protein kinase activities (ATP:protein phosphotransferase, EC 2.7.1.37) associated with p80 and p90. These protein kinase activities were found to be functionally indistinguishable but could be easily distinguished from the activities associated with PRCII p105 and FSV p140 on the basis of their cation requirement and target site specificity. On that basis also, p80/p90-associated protein kinases were found to be more similar to the enzymatic activity of pp60src than to those associated with the PRCII and FSV transformation-specific polyproteins. These results document a close genetic relationship between the two independently isolated sarcoma viruses Y73 and ESV. On the basis of the relatedness of transformation-specific proteins, ESV and Y73 constitute class III of avian sarcoma viruses, with class I containing the various strains of RSV and class II encompassing FSV and PRCII.

Alpharetrovirus↗
PubMed1985

Preferential lymphocyte-mediated cytotoxicity of syngeneic target cells in chickens bearing tumors induced by avian sarcoma virus.

Splenic lymphocytes from chickens bearing tumors induced by avian sarcoma virus are able to cause the specific killing of cultured avian sarcoma cells. This cytotoxicity appears to follow classical patterns of syngeneic restriction. Little or no specific killing of tumor targets occurred when spleen cells from one inbred line of chickens were tested against allogeneic targets, although syngeneic killing proceeded relatively efficiently. Other patterns of immune reactivity did not appear to be syngeneically restricted. Namely, sera from tumor-bearing hosts were equally reactive in indirect immunofluorescence assays with syngeneic and allogeneic target cells. And, peripheral blood lymphocytes from sensitized hosts could be stimulated equally well by tumor cell culture fluids of allogeneic or syngeneic origin.

Animals↗