Simian virus 40 facilitates multiplication of replication defective mutants of polyoma virus in BALB/3T3 mouse cells

Nature ◽  
1977 ◽  
Vol 267 (5611) ◽  
pp. 528-529 ◽  
Author(s):  
AKIRA HAKURA
1983 ◽  
Vol 3 (1) ◽  
pp. 1-8 ◽  
Author(s):  
E W Khandjian ◽  
H Türler

During the lytic infection of monkey and mouse cells with simian virus 40 and polyoma virus, respectively, the preferentially increased synthesis of two host proteins of 92,000 and 72,000 Mr was observed by 15 to 20 h after infection besides the general stimulation of most cellular proteins. The incubation of uninfected monkey and mouse cell cultures for 30 to 60 min at 43.5 degrees C induced the enhanced synthesis of at least three proteins of 92,000, 72,000 and 70,000 Mr, the last one being the major heat shock protein of mammalian cells. Two-dimensional gel electrophoresis and partial proteolytic digestion confirmed that the same 92,000- and 72,000-Mr proteins are stimulated by virus infection and thermal treatment. In simian virus 40-infected CV-1 cells, we also observed the weak stimulation of a 70,000-Mr protein comigrating in gel electrophoresis with the major heat shock protein. The 92,000-, 72,000- and 70,000-Mr proteins of monkey cells are structurally very similar to the corresponding proteins of mouse cells. In immunoprecipitations, no specific association of these proteins to simian virus 40 T antigens was noticed.


1983 ◽  
Vol 3 (1) ◽  
pp. 1-8
Author(s):  
E W Khandjian ◽  
H Türler

During the lytic infection of monkey and mouse cells with simian virus 40 and polyoma virus, respectively, the preferentially increased synthesis of two host proteins of 92,000 and 72,000 Mr was observed by 15 to 20 h after infection besides the general stimulation of most cellular proteins. The incubation of uninfected monkey and mouse cell cultures for 30 to 60 min at 43.5 degrees C induced the enhanced synthesis of at least three proteins of 92,000, 72,000 and 70,000 Mr, the last one being the major heat shock protein of mammalian cells. Two-dimensional gel electrophoresis and partial proteolytic digestion confirmed that the same 92,000- and 72,000-Mr proteins are stimulated by virus infection and thermal treatment. In simian virus 40-infected CV-1 cells, we also observed the weak stimulation of a 70,000-Mr protein comigrating in gel electrophoresis with the major heat shock protein. The 92,000-, 72,000- and 70,000-Mr proteins of monkey cells are structurally very similar to the corresponding proteins of mouse cells. In immunoprecipitations, no specific association of these proteins to simian virus 40 T antigens was noticed.


1981 ◽  
Vol 38 (3) ◽  
pp. 940-951 ◽  
Author(s):  
M Lange ◽  
E May ◽  
P May

1982 ◽  
Vol 79 (6) ◽  
pp. 2064-2067 ◽  
Author(s):  
V. B. Reddy ◽  
S. S. Tevethia ◽  
M. J. Tevethia ◽  
S. M. Weissman

1986 ◽  
Vol 6 (11) ◽  
pp. 4130-4132 ◽  
Author(s):  
S Hayashi ◽  
H Kondoh

Expression of the chicken delta-crystallin gene 1 injected into the nuclei of mouse cells is lens specific. Coinjection of GC box-containing DNA fragments from delta-crystallin, simian virus 40 early, and herpes simplex virus type 1 tk promoters effectively suppressed delta-crystallin expression in the lens, but coinjection with DNA fragments not containing the GC box did not. This suppression was likely due to the competition of an Sp1-like transcription factor(s) and indicates involvement of the apparently ubiquitous factor(s) in the tissue-specific expression of the delta-crystallin gene.


1973 ◽  
Vol 11 (6) ◽  
pp. 1027-1029
Author(s):  
Robert E. Gallagher ◽  
Arthur S. Levine ◽  
David H. Gillespie ◽  
Robert C. Gallo

Virology ◽  
1980 ◽  
Vol 107 (2) ◽  
pp. 488-496 ◽  
Author(s):  
Satvir S. Tevethia ◽  
David C. Flyer ◽  
Mary J. Tevethia ◽  
William C. Topp

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