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[Characteristic of the two-step RNA dimerization in avian sarcoma and leukosis viruses].

Dimerization of two copies of genomic RNA is a necessary step of retroviral replication. In the case of human immunodeficiency virus type 1 (HIV-1) the process is explored in many details. It is proved that conserved stem-loop structure is an essential element in RNA dimerization. Similar model of two-step dimerization mechanism can be considered for avian sarcoma and leukosis virus group (ASLV) in spite of the absence of homology between dimer initiation site (DIS) of ASLV and that of HIV-1. In this paper, short RNA fragments of two viruses: avian sarcoma virus CT-10 and avian leukosis virus HPRS-103 have been chosen in order to investigate the structural requirements of dimerization process and compare them to that of HIV-1. The rate of spontaneous transition from loose to tight dimer was studied as a function of stem length and temperature. Although both types of dimers were observed for both avian retroviruses chosen, fragments of CT-10 requires much higher RNA concentration to form loose dimer. In spite of identical sequence of the loops (5'-A-CUGCAG-3') avian sarcoma virus CT-10 RNA fragments dimerization was greatly impaired. The differences can be explained by deletion of adenine 271 in avian sarcoma virus CT-10 in the stem and by resulting shortening of the self-complementary loop.

Animals↗

PubMed1979

Immune response to the src gene product in mice bearing tumors induced by injection of avian sarcoma virus-transformed mouse cells.

A single subcutaneous injection of 10(7) live cells of the highly tumorigenic avian sarcoma virus (Schmidt-Ruppin strain, subgroup D)-transformed BALB/c line into BALB/c mice resulted in the production of an antiserum specific for the avian sarcoma virus gene product pp60src. All sera taken from mice 3 weeks after injection of tumor cells contained antibodies to pp60src. Immunoprecipitation experiments showed that all sera precipitated pp60src from Schmidt-Ruppin-infected chicken cells, but only a portion of these sera precipitated pp60src from chicken cells infected with other strains of avian sarcoma virus, i.e., Prague and Bratislava-77. Analysis of the cross-reactivity patterns of these antisera demonstrated a minimum of three to four antigenic determinants on pp60src. The findings reported here should facilitate the production of monoclonal antibodies to pp60src, which in turn will provide highly specific probes for further investigations into the structure and function of this protein.

Animals↗

PubMed1983

Isolation and partial purification of a new class of transforming growth factors from an avian sarcoma virus-transformed rat cell line.

Transformation of rat cells by avian sarcoma viruses induced the release of growth factors into serum-free conditioned medium. An avian sarcoma virus-transformed rat cell line, 77N1, produced and released a polypeptide growth factor, classified as a transforming growth factor (TGF), which transiently promotes anchorage-dependent BALB3T3 A31 cells to form progressively growing colonies in soft agar. The TGF was isolated and partially purified from an extract of 77N1 cells by ion-exchange chromatography on a diethylaminoethyl Sephacel column followed by ammonium sulfate precipitation. The TGF was assumed to have a molecular weight of 11,000 from gel filtration on Sephadex G-50. This TGF did not compete with epidermal growth factor for binding to cell membrane receptors and was not potentiated by epidermal growth factor. The TGF was trypsin and dithiothreitol sensitive as well as heat and acid labile, indicating that it was different from previously reported TGFs of similar molecular weight and thus belonged to a new class of TGFs.

Animals↗

PubMed2004

Two different molecular defects in the Tva receptor gene explain the resistance of two tvar lines of chickens to infection by subgroup A avian sarcoma and leukosis viruses.

The subgroup A to E avian sarcoma and leukosis viruses (ASLVs) are highly related and are thought to have evolved from a common ancestor. These viruses use distinct cell surface proteins as receptors to gain entry into avian cells. Chickens have evolved resistance to infection by the ASLVs. We have identified the mutations responsible for the block to virus entry in chicken lines resistant to infection by subgroup A ASLVs [ASLV(A)]. The tva genetic locus determines the susceptibility of chicken cells to ASLV(A) viruses. In quail, the ASLV(A) susceptibility allele tva(s) encodes two forms of the Tva receptor; these proteins are translated from alternatively spliced mRNAs. The normal cellular function of the Tva receptor is unknown; however, the extracellular domain contains a 40-amino-acid, cysteine-rich region that is homologous to the ligand binding region of the low-density lipoprotein receptor (LDLR) proteins. The chicken tva(s) cDNAs had not yet been fully characterized; we cloned the chicken tva cDNAs from two lines of subgroup A-susceptible chickens, line H6 and line 0. Two types of chicken tva(s) cDNAs were obtained. These cDNAs encode a longer and shorter form of the Tva receptor homologous to the Tva forms in quail. Two different defects were identified in cDNAs cloned from two different ASLV(A)-resistant inbred chickens, line C and line 7(2). Line C tva(r) contains a single base pair substitution, resulting in a cysteine-to-tryptophan change in the LDLR-like region of Tva. This mutation drastically reduces the binding affinity of Tva(R) for the ASLV(A) envelope glycoproteins. Line 7(2) tva(r2) contains a 4-bp insertion in exon 1 that causes a change in the reading frame, which blocks expression of the Tva receptor.

Amino Acid Sequence↗

PubMed1980

In vivo effect of three transformation-defective mutants of subgroup C avian sarcoma viruses.

Three transformation-defective mutants derived from avian sarcoma viruses of subgroup C, td PR-RSV-C (Vogt), td B77 (Toyoshima) and td daPR-RSV-C (isolated in our laboratory), were injected intravenously into 12-day-old chicken embryos and intraperitoneally into newly-hatched chickens. Both Brown Leghorn chickens and F1 hybrids of two inbred chicken lines (C X I) were used. Haematological changes and formation of visible tumours were evaluated in animals kept for 8-9 months. All three td mutants produced in a significant proportion of intraembryonally injected animals haematological disorders which, in certain cases, resembled the anaemic and proliferative type of erythroblastosis. Most conspicuous symptoms of erythroblastosis were seen after td daPR-RSV-C which also gave rise to two sarcomas, containing transforming viruses. The possible character of oncogenic information retained or acquired by the TD mutants is discussed.

Anemia↗

PubMed1984

Characteristics of three new avian sarcoma viruses, ASV 9, ASV 17, and ASV 25.

Three new avian sarcoma viruses, ASV 9, ASV 17, and ASV 25, were isolated from spontaneous tumors. They transform chicken embryo fibroblasts but not hemopoietic cells and induce fibrosarcomas in young chicks. All three viruses belong to the envelope subgroup A and cannot replicate without a helper virus, because they lack the pol and most, if not all, of the env gene. ASV 9 and ASV 17 have a genome of 5.0 kb; the genome of ASV 25 is 6.0 kb. The following onc sequences were tested for homology to the genomes of the three new avian sarcoma viruses: src, fps, yes, myc, myb, erbA, and erbB. These tests were negative except for erbB which showed faint hybridization with the genome of ASV 25. ASV 9 codes for a prominent 130-kdalton gag-linked transformation-specific protein. ASV 17 and ASV 25 transformed cells appear to contain multiple gag-linked transformation-specific proteins that still require further study.

Animals↗

PubMed1979

Decreased production of transforming virus and altered antigenic behaviour in cultured avian sarcoma cells.

Tumours induced in chickens by inoculation of avian sarcoma viruses are frequently capable of undergoing spontaneous regression. It is only those tumour cells which have been derived from progressively growing neoplasms that are able to produce transforming progeny virus in vitro and to shed into the culture medium antigens which are specifically reactive with the peripheral lymphocytes of sarcoma-bearing hosts. Following multiple passages and extended growth in culture, however, the ability of these tumour cell fluids to stimulate the lymphocytes of sensitized hosts diminishes in concert with the declining capacity of these cells to continue to synthesize fully transforming progeny virus. In certain instances, however, aged tumour cells are able to synthesize particles which contain the enzyme RNA-dependent DNA polymerase yet lack detectable envelope glycoprotein.

Animals↗

PubMed1978

General immunocompetence of rats bearing avian sarcoma virus-induced intracranial tumors.

The mitogenic responsiveness of spleen cells obtained from avian sarcoma virus-inoculated Fischer 344 rats was studied. Sixty % of the rats had astrocytomas, 13% had sarcomas, 7% had mixed gliosarcomas, and 20% had no evidence of tumors. Only spleen cells from rats bearing astrocytomas had significantly diminished responses to phytohemagglutinin and concanavalin A (Con A) when compared to control responses. The decreased responsiveness observed with phytohemagglutinin was limited to the optimal concentration range (10 and 20 microgram) while a broader concentration of Con A (0.01 to 50 microgram) induced significant suppression. Moreover, a more profound immunosuppression was observed with Con A. The results also demonstrated that spleen cells from rats with the largest astrocytomas exhibited the greatest suppression. From the results of this study, it appears the avian sarcoma virus-induced astrocytoma in rats is an immunological parallel of the human disease based on the loss of general immunological competence as assessed by responsiveness of lymphocytes to phytohemagglutinin and Con A.

Alpharetrovirus↗

PubMed1982

Experimental allergic encephalomyelitis in Lewis rats bearing avian sarcoma virus-induced brain tumors.

Lewis rats bearing avian sarcoma virus (ASV)-induced brain tumors were injected with guinea pig spinal cord emulsion and complete Freund's Adjuvant to determine if they remained susceptible to induction of experimental allergic encephalomyelitis (EAE). The incidence of EAE among rats with small, and moderate sized gliomas was similar to non-tumor-bearing controls (P less than 0.5; P less than 0.9) while 18 of 24 (75%) animals with large gliomas developed EAE as compared to 31 of 33 (93%) controls (P less than 0.05). The histologic features and geographical distribution of "ordinary' EAE were seen in controls and were maintained in tumor-bearing rats. The presence of an intracranial tumor did not significantly alter the ability of Lewis rats to develop EAE.

Animals↗

PubMed1976

Suppression of the avian sarcoma virus genome in 8-azaquanine-resistant, transformed, hamster cells.

The avian sarcoma virus genome (Schmidt-Ruppin strain) in transformed hamster cells resistant to 8-azaquanine [Ha(SR)AG-50] was strongly suppressed. The suppression was genetically stable and could not be overcome by attempts at induction with 5-iodo-2'-deoxyuridine. Fusion of hamster cells, which had suppressed virus genome, with chicken Rous-associated virus (RAV-1)-preinfected cells easily rescued the sarcoma virus. The rescued virus had envelope properties of RAV-1, as determined by viral interference, virus neutralization, and plating on genetically resistant chicken cells. By repeatedly cloning the rescued virus, we determined that virus recombined in the rescue experiment and that the recombinant virus had the envelope properties of helper virus used for its rescue. Cells with suppressed avian sarcoma virus genome were suitable for preparation of different recombinant viruses.

Animals↗

PubMed1977

Terminally repeated sequences in the avian sarcoma virus RNA genome.

The initiation of DNA synthesis in vitro by RNA-directed DNA polymerase (deoxynucleosidetriphosphate: DNA deoxynucleotidyltransferase, EC 2.7.7.7) of avian oncornaviruses requires a tRNAtrp primer molecule located close to the 5' end of the viral RNA genome. DNA transcripts, 100 nucleotides in length, initiated on the tRNAtrp primer molecule contain nucleotide sequences complementary to a large (25 nucleotides) RNase T1 oligonucleotide, T-13, located at the 5' terminus of the avian sarcoma virus RNA genome. tRNAtrp-initiated DNA transcripts with a length of about 70 nucleotides contain substantially fewer nucleotide sequences complementary to this 5'-terminal oligonucleotide, suggesting that the tRNAtrp primer associated with the avian sarcoma virus RNA is located approximately 100 nucleotides from the 5' end of the RNA. In addition, we present evidence to demonstrate that DNA transcribed from avian sarcoma virus RNA sequences located at the 3' end, immediately adjacent to the poly(A), contains nucleotide sequences that are complementary to the 5'-terminal T1 oligonucleotide T-13. These data indicate that the 5' end of the viral genome contains nucleotide sequences that are repeated at the 3' end of the genome. We conclude that the avian oncornavirus RNA genome is terminally redundant.

Avian Sarcoma Viruses↗

PubMed1981

Synthesis of plus strands of retroviral DNA in cells infected with avian sarcoma virus and mouse mammary tumor virus.

The vast majority of plus strands synthesized in quail cells acutely infected with avian sarcoma virus were subgenomic in size, generally less than 3 kilobases (kb). A series of discrete species could be identified after agarose gel electrophoresis by annealing with various complementary DNAs, indicating specificity in the initiation and termination of plus strands. The first plus strand to appear (within 2 h postinfection) was similar in length to the long redundancy at the ends of linear DNA (0.35 kb), and it annealed with complementary DNAs specific for the 3' and 5' termini of viral RNA (Varmus et al., J. Mol. Biol. 120:50-82, 1978). Several subgenomic plus-strand fragments (0.94, 1.38, 2.3, and 3.4 kb) annealed with these reagents. At least the 0.94- and 1.38-kb strands were located at the same end of linear DNA as the 0.35-kb strand, indicating that multiple specific sites for initiation were employed to generate strands which overlapped on the structural map. We were unable to detect RNA liked to plus strands isolated as early as 2.5 h postinfection; thus, the primers must be short (fewer than 50 to 100 nucleotides), rapidly removed, or not composed of RNA. To determine whether multiple priming events are a general property of retroviral DNA synthesis in vivo, we also examined plus strands of mouse mammary tumor virus DNA in chronically infected rat cells after induction of RNA and subsequent DNA synthesis with dexamethasone. In this case, multiple, discrete subgenomic DNA plus strands were not found when the same methods applied to avian sarcoma virus DNA were used; instead, the plus strands present in the linear DNA of mouse mammary tumor virus fell mainly into two classes: (i) strands of ca. 1.3 kb which appeared early in synthesis and were similar in size and genetic content to the terminally repeated sequence in linear DNA; and (ii) plus strands of the same length as linear DNA. A heterogeneous population of other strands diminished with time, was not found in completed molecules, and was probably composed of strands undergoing elongation. These two retroviruses thus appear to differ with respect to both the number of priming sites used for the synthesis of plus strands and the abundance of full-length plus strands. On the other hand the major subgenomic plus strand of mouse mammary tumor virus DNA (1.3 kb) is probably the functional homolog of a major subgenomic plus strand of avian sarcoma virus DNA (0.35 kb). The significance of this plus strand species is discussed in the context of current models which hold that it is used as a template for the completion of the minus strand, thereby generating the long terminal redundancy.

Animals↗

PubMed1983

Localization of active promoters for eucaryotic RNA polymerase II in the long terminal repeat of avian sarcoma virus DNA.

The nucleotide sequences in the long terminal repeat of avian sarcoma virus that are recognized in vitro by HeLa cell RNA polymerase II have been identified. For this purpose, various 5' and 3' deletions were introduced into a cloned long terminal repeat fragment. The effects of these deletions on transcription initiation in HeLa whole-cell extracts were then studied. Three specific transcripts have been identified. The major transcript is initiated at nucleotide +1 (relative to the cap site). Deletion of the upstream sequence between -299 and -55 has no effect on the level of transcription from this start site, whereas deletion of the sequence downstream of -14 drastically reduces the levels of transcription. In contrast, deletion of the sequence downstream from the TATA box has no effect on the initiation or efficiency of synthesis of the two minor RNA species, which are initiated at around nucleotides -260 and -105. The transcription of these RNA products, however, is abolished by an upstream deletion between -299 and -55. These results suggest that HeLa cell RNA polymerase II recognizes in vitro more than one promoter site present in the long terminal repeat of the avian sarcoma virus genome and defines the sequences required for initiation of the major transcript.

Avian Sarcoma Viruses↗

PubMed1978

Avian myelocytomatosis and erythroblastosis viruses lack the transforming gene src of avian sarcoma viruses.

Using labeled cDNA specific for the detection of the src gene of avian sarcoma viruses, we find that avian myelocytomatosis virus strain MC29 and avian erythroblastosis virus strain ES4 lack nucleotide sequences related to the src gene. Furthermore, chicken fibroblasts as well as hematopoietic cells, infected and transformed with these viruses, show no enhanced level of transcription of the cellular nucleotide sequences related to the src gene of avian sarcoma viruses. These two viruses may thus contain their own transforming gene(s) or induce cellular genes unrelated to the src-like cellular sequences.

Alpharetrovirus↗

PubMed1985

Generation of a recombinant Moloney murine leukemia virus carrying the v-src gene of avian sarcoma virus: transformation in vitro and pathogenesis in vivo.

A Moloney murine leukemia virus (M-MuLV) recombinant carrying the v-src gene of avian sarcoma virus was generated by the introduction of a cloned portion of v-src from Schmidt-Ruppin A avian sarcoma virus into a molecular clone of M-MuLV provirus at the recombinant DNA level. The v-src sequences (lacking a portion of the 5' end of v-src) were inserted into the p30 region of the M-MulV gag gene so that M-MuLV gag and v-src were in the same reading frame. Transfection of this chimeric clone, pMLV(src), into NIH 3T3 cells which were constitutively producing M-MuLV gag and pol protein resulted in the formation of foci of transformed cells. Infectious and transforming virus could be recovered from the transformed cells. This virus was designated M-MuLV(src). M-MuLV(src)-transformed cells contained two novel proteins of 78 and 90 kilodaltons. The 78-kilodalton protein, p78gag-src, contained both gag and src determinants, exhibited kinase activity in an immune kinase assay, and is probably a fusion of Pr65gag and src. The 90-kilodalton protein, which is of the appropriate size to be the gPr80gag fused to src, contained gag determinants as well as a V8 protease cleavage fragment typical of the carboxy terminus of avian sarcoma virus pp60src. However, it could not be immunoprecipitated with an anti-v-src serum. M-MuLV(src)-transformed cells showed elevated levels of intracellular phosphotyrosine in proteins, although the elevation was intermediate compared with cells transformed with wild-type v-src. M-MuLV and amphotropic murine leukemia virus pseudotypes of M-MuLV(src) were inoculated into newborn NIH Swiss mice. Inoculated mice developed solid tumors at the site of inoculation after 3 to 6 weeks, with most animals dying by 14 weeks. Histopathological analysis indicated that the solid tumors were mesenchymally derived fibrosarcomas that were both invasive and metastatic.

Amino Acids↗

PubMed1980

Identification of a cellular protein substrate phosphorylated by the avian sarcoma virus-transforming gene product.

The avian sarcoma virus-transforming gene product (pp60src) appears potentially able to mediate cell transformation via phosphorylation since it is tightly associated with a protein kinase activity. We have searched for and have been able to identify a normal cellular protein that appears to be a substrate of pp60src. The phosphorylation of this protein (34K) in transformation-specific in ASV-transformed cells of both avian and mammalian origin. Moreover, the 34K polypeptide serves as a substrate for the pp60src phosphotransferase activity in vitro and is phosphorylated at a site identical to the major site of phosphorylation in vivo. These data suggest that upon transformation the 34,000-dalton protein is phosphorylated directly as a result of pp60src activity.

Animals↗

PubMed1986

Modification of carboxyl-terminal region is the cause of activation of the src gene in avian sarcoma virus S2.

Viral oncogene product of avian sarcoma virus S2 was reported to have two alterations from proto-src product; a substitution of its extreme carboxyl terminus with a peptide of helper viral protein and a point mutation which altered the 501st amino acid from arginine to lysine. However, the following data suggest that lysine501 is more common in proto-src product than arginine501. Proto-src from two independent embryos which we analyzed encoded lysine for the 501st amino acid. Rous sarcoma virus and S1, another isolate which had transduced proto-src, also coded for lysine at the same position. Thus, in the case of S2, the oncogenic activation of the src gene appeared to be achieved with only an alteration at its carboxyl terminus and enhanced expression by long terminal repeats.

Amino Acid Sequence↗

PubMed1982

Oncogene and its production of an avian sarcoma virus Y73.

The Y73 strain of avian sarcoma virus isolated from a transplantable chicken tumor was defective in its replicating capacity. The virus caused sarcoma but not acute leukosis in chickens even when inoculated intravenously. It induced transformed cell-foci in cultured fibroblasts and the viral genome responsible for in vitro transformation was 26S RNA. The RNA was composed of sequences in common with helper virus RNA and Y73-specific sequence. The specific sequence "yes" did not hybridize with complementary DNA to the src gene of Rous sarcoma virus (cDNAsrc) and it had a unique counterpart in normal cell DNA. The yes gene was located in the middle of the 26S genome and the sequences common to the helper virus were located toward both ends. The 26S RNA coded for an polyprotein of 90,000 daltons (p90) which included p19 of viral core proteins in addition to the polypeptide unique to the yes gene. p90 had protein kinase activity specific for tyrosine residue and itself could be phosphorylated at tyrosine residue in vivo and in vitro, and at serine residue in vivo.

Animals↗