Adenosylhomocysteine hydrolase inhibitors: Synthesis of 5′-deoxy-5′-(isobutylthio)-3-deazaadenosine and its effect on Rous sarcoma virus and Gross murine leukemia virus

1978 ◽  
Vol 82 (2) ◽  
pp. 417-423 ◽  
Author(s):  
Peter K. Chiang ◽  
Giulio L. Cantoni ◽  
John P. Bader ◽  
William M. Shannon ◽  
H.Jeanette Thomas ◽  
...  
Keyword(s):  
Murine Leukemia Virus ◽  
Rous Sarcoma Virus ◽  
Leukemia Virus ◽  
Adenosylhomocysteine Hydrolase ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Murine Leukemia

scholarly journals Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins.

1981 ◽  
Vol 1 (5) ◽  
pp. 394-407 ◽  
Author(s):  
J A Cooper ◽  
T Hunter
Keyword(s):  
Murine Leukemia Virus ◽  
Rous Sarcoma Virus ◽  
Leukemia Virus ◽  
Specific Protein ◽  
Cellular Proteins ◽  
3T3 Cells ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Abelson Murine Leukemia Virus ◽  
Murine Leukemia

Chicken embryo cells transformed by the related avian sarcoma viruses PRC II and Fujinami sarcoma virus, or by the unrelated virus Y73, contain three phosphoproteins not observed in untransformed cells and increased levels of up to four other phosphoproteins. These same phosphoproteins are present in increased levels in cells transformed by Rous sarcoma virus, a virus which is apparently unrelated to the three aforementioned viruses. In all cases, the phosphoproteins contain phosphotyrosine and thus may be substrates for the tyrosine-specific protein kinases encoded by these viruses. In one case, the site(s) of tyrosine phosphorylation within the protein is the same for all four viruses. A homologous protein is also phosphorylated, at the same major site, in mouse 3T3 cells transformed by Rous sarcoma virus or by the further unrelated virus Abelson murine leukemia virus. A second phosphotyrosine-containing protein has been detected in both Rous sarcoma virus and Abelson murine leukemia virus-transformed 3T3 cells, but was absent from normal 3T3 cells and 3T3 cells transformed by various other viruses. We conclude that representatives of four apparently unrelated classes of transforming retroviruses all induce the phosphorylation of tyrosines present in the same set of cellular proteins.

Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins

1981 ◽  
Vol 1 (5) ◽  
pp. 394-407
Author(s):  
J A Cooper ◽  
T Hunter
Keyword(s):  
Murine Leukemia Virus ◽  
Rous Sarcoma Virus ◽  
Leukemia Virus ◽  
Specific Protein ◽  
Cellular Proteins ◽  
3T3 Cells ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Abelson Murine Leukemia Virus ◽  
Murine Leukemia

Chicken embryo cells transformed by the related avian sarcoma viruses PRC II and Fujinami sarcoma virus, or by the unrelated virus Y73, contain three phosphoproteins not observed in untransformed cells and increased levels of up to four other phosphoproteins. These same phosphoproteins are present in increased levels in cells transformed by Rous sarcoma virus, a virus which is apparently unrelated to the three aforementioned viruses. In all cases, the phosphoproteins contain phosphotyrosine and thus may be substrates for the tyrosine-specific protein kinases encoded by these viruses. In one case, the site(s) of tyrosine phosphorylation within the protein is the same for all four viruses. A homologous protein is also phosphorylated, at the same major site, in mouse 3T3 cells transformed by Rous sarcoma virus or by the further unrelated virus Abelson murine leukemia virus. A second phosphotyrosine-containing protein has been detected in both Rous sarcoma virus and Abelson murine leukemia virus-transformed 3T3 cells, but was absent from normal 3T3 cells and 3T3 cells transformed by various other viruses. We conclude that representatives of four apparently unrelated classes of transforming retroviruses all induce the phosphorylation of tyrosines present in the same set of cellular proteins.

scholarly journals Infection of Nondividing Cells by Rous Sarcoma Virus

2001 ◽  
Vol 75 (19) ◽  
pp. 9526-9531 ◽  
Author(s):  
Theodora Hatziioannou ◽  
Stephen P. Goff
Keyword(s):  
Human Immunodeficiency Virus ◽  
Murine Leukemia Virus ◽  
Rous Sarcoma Virus ◽  
Leukemia Virus ◽  
Viral Dna ◽  
Rous Sarcoma ◽  
Immunodeficiency Virus ◽  
Sarcoma Virus ◽  
Murine Leukemia

ABSTRACT A direct comparison demonstrates that Rous sarcoma virus is capable of infecting aphidicolin-arrested cells 10-fold more efficiently than murine leukemia virus but less efficiently than human immunodeficiency virus. The efficiency of infection of nondividing cells by the three viruses correlates with the respective ability of each viral DNA to enter the nucleus.

scholarly journals Conditions for Copackaging Rous Sarcoma Virus and Murine Leukemia Virus Gag Proteins during Retroviral Budding

1999 ◽  
Vol 73 (3) ◽  
pp. 2045-2051 ◽  
Author(s):  
Robert P. Bennett ◽  
John W. Wills
Keyword(s):  
Plasma Membrane ◽  
Murine Leukemia Virus ◽  
Rous Sarcoma Virus ◽  
Sequence Similarity ◽  
Leukemia Virus ◽  
Particle Assembly ◽  
Gag Proteins ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Murine Leukemia

ABSTRACT Rous sarcoma virus (RSV) and murine leukemia virus (MLV) are examples of distantly related retroviruses that normally do not encounter one another in nature. Their Gag proteins direct particle assembly at the plasma membrane but possess very little sequence similarity. As expected, coexpression of these two Gag proteins did not result in particles that contain both. However, when the N-terminal membrane-binding domain of each molecule was replaced with that of the Src oncoprotein, which is also targeted to the cytoplasmic face of the plasma membrane, efficient copackaging was observed in genetic complementation and coimmunoprecipitation assays. We hypothesize that the RSV and MLV Gag proteins normally use distinct locations on the plasma membrane for particle assembly but otherwise have assembly domains that are sufficiently similar in function (but not sequence) to allow heterologous interactions when these proteins are redirected to a common membrane location.

scholarly journals Mutations in the Spacer Peptide and Adjoining Sequences in Rous Sarcoma Virus Gag Lead to Tubular Budding

2008 ◽  
Vol 82 (14) ◽  
pp. 6788-6797 ◽  
Author(s):  
Paul W. Keller ◽  
Marc C. Johnson ◽  
Volker M. Vogt
Keyword(s):  
Rous Sarcoma Virus ◽  
Mutational Analysis ◽  
Leukemia Virus ◽  
Alpha Helix ◽  
Insertion Mutagenesis ◽  
Structural Protein ◽  
Enveloped Virus ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Hiv 1

ABSTRACT All orthoretroviruses encode a single structural protein, Gag, which is necessary and sufficient for the assembly and budding of enveloped virus-like particles from the cell. The Gag proteins of Rous sarcoma virus (RSV) and human immunodeficiency virus type 1 (HIV-1) contain a short spacer peptide (SP or SP1, respectively) separating the capsid (CA) and nucleocapsid (NC) domains. SP or SP1 and the residues immediately upstream are known to be critical for proper assembly. Using mutagenesis and electron microscopy analysis of insect cells or chicken cells overexpressing RSV Gag, we defined the SP assembly domain to include the last 8 residues of CA, all 12 residues of SP, and the first 4 residues of NC. Five- or two-amino acid glycine-rich insertions or substitutions in this critical region uniformly resulted in the budding of abnormal, long tubular particles. The equivalent SP1-containing HIV-1 Gag sequence was unable to functionally replace the RSV sequence in supporting normal RSV spherical assembly. According to secondary structure predictions, RSV and HIV-1 SP/SP1 and adjoining residues may form an alpha helix, and what is likely the functionally equivalent sequence in murine leukemia virus Gag has been inferred by mutational analysis to form an amphipathic alpha helix. However, our alanine insertion mutagenesis did not provide evidence for an amphipathic helix in RSV Gag. Taken together, these results define a short assembly domain between the folded portions of CA and NC, which is essential for formation of the immature Gag shell.

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