Analysis of Adhesion Plaque Structure and Function in the Mechanism of Transformation by Rous Sarcoma Virus

1982 ◽  
Vol 40 ◽  
pp. 110-113
Author(s):  
L.R. Rohrschneider ◽  
M.J. Rosok ◽  
L.E. Gentry
Keyword(s):  
Rous Sarcoma Virus ◽  
Mammalian Cells ◽  
Neoplastic Transformation ◽  
Structure And Function ◽  
Excellent Opportunity ◽  
Cells In Culture ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
And Function ◽  
Adhesion Plaque

Rous sarcoma virus (RSV) was originally isolated from a fibrosarcoma of a chicken. This virus also will efficiently infect and transform all avian cells in culture as well as most mammalian cells. The mechanism of transformation by RSV is therefore universal and this system offers an excellent opportunity to investigate the mechanism of neoplastic transformation.

Effects of Rous Sarcoma Virus on the Differentiation of Chick and Quail Neuroretina Cells in Culture

1982 ◽  
pp. 115-122 ◽  
Author(s):  
Patricia Crisanti-Combes ◽  
Anne-Marie Lorinet ◽  
Arlette Girard ◽  
Bernard Pessac ◽  
Marion Wasseff ◽  
...  
Keyword(s):  
Rous Sarcoma Virus ◽  
Cells In Culture ◽  
Rous Sarcoma ◽  
Sarcoma Virus

scholarly journals A Variant Schmidt-Ruppin Strain of Rous Sarcoma Virus with Increased Affinity for Mammalian Cells

1989 ◽  
Vol 80 (12) ◽  
pp. 1179-1185 ◽  
Author(s):  
Sadaaki Kawai ◽  
Makoto Nishizawa ◽  
Hideko Shinno-Kohno ◽  
Kazuko Shiroki
Keyword(s):  
Rous Sarcoma Virus ◽  
Mammalian Cells ◽  
Rous Sarcoma ◽  
Sarcoma Virus

scholarly journals Cryo-EM structure of the Rous sarcoma virus octameric cleaved synaptic complex intasome

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Krishan K. Pandey ◽  
Sibes Bera ◽  
Ke Shi ◽  
Michael J. Rau ◽  
Amarachi V. Oleru ◽  
...  
Keyword(s):  
Rous Sarcoma Virus ◽  
Single Amino Acid ◽  
Strand Transfer ◽  
Synaptic Complex ◽  
Rous Sarcoma ◽  
Tetrameric Structure ◽  
Sarcoma Virus ◽  
And Function ◽  
Key Steps

AbstractDespite conserved catalytic integration mechanisms, retroviral intasomes composed of integrase (IN) and viral DNA possess diverse structures with variable numbers of IN subunits. To investigate intasome assembly mechanisms, we employed the Rous sarcoma virus (RSV) IN dimer that assembles a precursor tetrameric structure in transit to the mature octameric intasome. We determined the structure of RSV octameric intasome stabilized by a HIV-1 IN strand transfer inhibitor using single particle cryo-electron microscopy. The structure revealed significant flexibility of the two non-catalytic distal IN dimers along with previously unrecognized movement of the conserved intasome core, suggesting ordered conformational transitions between intermediates that may be important to capture the target DNA. Single amino acid substitutions within the IN C-terminal domain affected intasome assembly and function in vitro and infectivity of pseudotyped RSV virions. Unexpectedly, 17 C-terminal amino acids of IN were dispensable for virus infection despite regulating the transition of the tetrameric intasome to the octameric form in vitro. We speculate that this region may regulate the binding of highly flexible distal IN dimers to the intasome core to form the octameric complex. Our studies reveal key steps in the assembly of RSV intasomes.

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