Viral products in cells infected with Vesicular Stomatitis virus and superinfected with Rous Sarcoma virus

1988 ◽  
Vol 100 (1-2) ◽  
pp. 121-129 ◽  
Author(s):  
M. Semmel ◽  
G. Mercier ◽  
N. Pavloff ◽  
G. Dambrine ◽  
F. Gay ◽  
...  
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Rous Sarcoma Virus ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Vesicular Stomatitis ◽  
In Cells

scholarly journals Late Domain Function Identified in the Vesicular Stomatitis Virus M Protein by Use of Rhabdovirus-Retrovirus Chimeras

1999 ◽  
Vol 73 (4) ◽  
pp. 3359-3365 ◽  
Author(s):  
Rebecca C. Craven ◽  
Ronald N. Harty ◽  
Jason Paragas ◽  
Peter Palese ◽  
John W. Wills
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Rous Sarcoma Virus ◽  
M Protein ◽  
Enveloped Viruses ◽  
Gag Proteins ◽  
Rous Sarcoma ◽  
M Proteins ◽  
Sarcoma Virus ◽  
Vesicular Stomatitis

ABSTRACT Little is known about the mechanisms used by enveloped viruses to separate themselves from the cell surface at the final step of budding. However, small sequences in the Gag proteins of several retroviruses (L domains) have been implicated in this process. A sequence has been identified in the M proteins of rhabdoviruses that closely resembles the PPPPY motif in the L domain of Rous sarcoma virus (RSV), an avian retrovirus. To evaluate whether the PPPY sequence in vesicular stomatitis virus (VSV) M protein has an activity analogous to that of the retroviral sequence, M-Gag chimeras were characterized. The N-terminal 74 amino acids of the VSV (Indiana) M protein, including the PPPY motif, was able to replace the L domain of RSV Gag and allow the assembly and release of virus-like particles. Alanine substitutions in the VSV PPPY motif severely compromised the budding activity of this hybrid protein but not that of another chimera which also contained the RSV PPPPY sequence. We conclude that this VSV sequence is functionally homologous to the RSV L domain in promoting virus particle release, making this the first example of such an activity in a virus other than a retrovirus. Both the RSV and VSV motifs have been shown to interact in vitro with certain cellular proteins that contain a WW interaction module, suggesting that the L domains are sites of interaction with unknown host machinery involved in virus release.

Identification of virus-specific RNA in cells infected with rous sarcoma virus

1971 ◽  
Vol 42 (5) ◽  
pp. 919-925 ◽  
Author(s):  
A.C. Garapin ◽  
J. Leong ◽  
L. Fanshier ◽  
W.E. Levinson ◽  
J.M. Bishop
Keyword(s):  
Rous Sarcoma Virus ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
In Cells

Membrane and cytoskeletal changes in cells after transformation by Rous Sarcoma virus

1987 ◽  
Vol 15 (5) ◽  
pp. 791-794 ◽  
Author(s):  
STUART KELLIE ◽  
NOEL M. WIGGLESWORTH ◽  
BIPIN PATEL ◽  
THOMAS C. HOLME ◽  
DAVID R. CRITCHLEY ◽  
...  
Keyword(s):  
Rous Sarcoma Virus ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
In Cells

scholarly journals Phosphorylation of cellular proteins in Rous sarcoma virus-infected cells: analysis by use of anti-phosphotyrosine antibodies.

1988 ◽  
Vol 8 (8) ◽  
pp. 3035-3042 ◽  
Author(s):  
M Hamaguchi ◽  
C Grandori ◽  
H Hanafusa
Keyword(s):  
Gel Electrophoresis ◽  
Rous Sarcoma Virus ◽  
Cellular Proteins ◽  
Morphological Transformation ◽  
Protein Substrates ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Infected Cells ◽  
Avian Sarcoma ◽  
In Cells

The protein substrates for the tyrosine protein kinases in cells transformed by avian sarcoma viruses were analyzed by gel electrophoresis in combination with immunoblotting or immunoprecipitation by antibodies against phosphotyrosine. We found that greater than 90% of phosphotyrosine-containing cellular proteins can be immunoprecipitated by these antibodies. The level of phosphotyrosine-containing cellular proteins detectable by this method markedly increased upon transformation with Rous sarcoma virus, and more than 20 distinct bands of such proteins were found in lysates of Rous sarcoma virus-transformed cells. Most of these phosphotyrosine-containing proteins had not been identified by other methods, and their presence appeared to correlate with morphological transformation in cells infected with various Rous sarcoma virus mutants and Y73, PRCII, and Fujinami sarcoma viruses. However, considerably different patterns were obtained with cells infected with nontransforming Rous sarcoma virus mutants that encode nonmyristylated src kinases, indicating that most substrates that correlate with transformation can only be recognized by p60v-src associated with the plasma membrane.

scholarly journals A glycoprotein in the plasma membrane matrix as a major potential substrate of p60v-src.

1990 ◽  
Vol 10 (2) ◽  
pp. 830-836 ◽  
Author(s):  
M Hamaguchi ◽  
M Matsuda ◽  
H Hanafusa
Keyword(s):  
Plasma Membrane ◽  
Rous Sarcoma Virus ◽  
Transmembrane Protein ◽  
Temperature Sensitive ◽  
Morphological Transformation ◽  
Fibronectin Receptor ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Potential Substrate ◽  
In Cells

A potential substrate of p60v-src in Rous sarcoma virus-transformed cells was found to be a 130-kilodalton (kDa) glycoprotein which binds to lectin-Sepharose and can be immunoprecipitated by an anti-phosphotyrosine antibody. This glycoprotein was shown to be distinct from the fibronectin receptor and a cellular protein phosphorylated in p60v-src immune complexes. The protein was a transmembrane protein localized in the plasma membrane and resistant to extraction with Triton X-100. The 130-kDa protein was also highly phosphorylated in cells transformed by Fujinami sarcoma virus or Y73 but not in cells infected with Rous sarcoma virus mutants that encode p60v-src lacking myristoylated N termini. Phosphorylation of this glycoprotein was temperature dependent in cells infected with temperature-sensitive mutants. The good correlation between its phosphorylation and morphological transformation, together with its relative abundance among phosphorylated proteins and its subcellular localization, suggests that phosphorylation of the 130-kDa glycoprotein is one of the primary events important for cell transformation by p60v-src and related oncogene products.

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