Thogoto and Dhori virus replication is blocked by inhibitors of cellular polymerase II activity but does not cause shutoff of host cell protein synthesis

1996 ◽  
Vol 141 (8) ◽  
pp. 1587-1594 ◽  
Author(s):  
J. Siebler ◽  
O. Haller ◽  
G. Kochs
Keyword(s):  
Protein Synthesis ◽  
Host Cell ◽  
Virus Replication ◽  
Cell Protein ◽  
Host Cell Protein

Transcriptional and translational events during reovirus infection

1988 ◽  
Vol 66 (8) ◽  
pp. 803-812 ◽  
Author(s):  
Guy Lemay
Keyword(s):  
Protein Synthesis ◽  
Host Cell ◽  
Mrna Translation ◽  
Cell Membrane Permeability ◽  
Cell Protein ◽  
Viral Mrna ◽  
Genomic Rna ◽  
Host Cell Protein ◽  
Outer Capsid ◽  
Viral Genomic Rna

This short review focuses on the mechanisms involved in transcription and translation in mouse L cells infected with reoviruses. The viral genomic RNA (double-stranded), retained in the inner capsid following removal of the outer capsid of the infecting virion, is transcribed by a viral polymerase. The synthesized viral mRNA is blocked at the 5′ end by a cap structure similar to the cap structure of cellular mRNA but synthesized by the viral enzymes of the inner capsid. This viral mRNA is also used as the first strand and template for the synthesis of the second strand of viral genomic RNA; the newly replicated genome is retained in an inner capsid structure to generate the progeny subviral particles. These particles are active at the transcriptional level but do not synthesize the cap, owing to the absence of the guanylyltransferase activity involved in the formation of this structure. The uncapped mRNA, or late viral mRNA, constitutes the bulk part of viral mRNA. The transcription of the viral genome is finally arrested upon addition of outer capsid proteins to obtain a mature virion. During viral multiplication, there is a gradual inhibition of host-cell protein synthesis, concomitant with stimulation of late viral mRNA translation. The two phenomena are apparently distinct. Furthermore, the inhibition of host-cell protein synthesis has been shown to be dispensable for normal virus multiplication; however, it might accelerate it. The mechanisms responsible for inhibition are still unclear but might involve modifications in the activity of cellular cap-binding proteins. This last point suggests an analogy with poliovirus infection; the two systems are thus briefly compared. Possible significance of the absence of a poly(A) tract at the 3′ end of reovirus mRNA, in contrast to the occurrence of such a sequence at the end of cellular mRNA, is also examined. Different models involving cap discrimination, competition between mRNAs, or alteration of cell membrane permeability have been proposed to explain the events observed at the translational level in reovirus-infected cells. These different models are compared. Finally, recent data implicating the viral sigma 3 capsid protein in efficient translation of late viral mRNA are discussed.

Initiation activity of EMC virus RNA, binding to initiation factor eIF-4B and shut-off of host cell protein synthesis

Nature ◽  
1978 ◽  
Vol 275 (5677) ◽  
pp. 240-243 ◽  
Author(s):  
CORRADO BAGLIONI ◽  
MARCELLA SIMILI ◽  
DAVID A. SHAFRITZ
Keyword(s):  
Protein Synthesis ◽  
Host Cell ◽  
Rna Binding ◽  
Initiation Factor ◽  
Cell Protein ◽  
Host Cell Protein ◽  
Virus Rna ◽  
Emc Virus

scholarly journals Mengovirus leader is involved in the inhibition of host cell protein synthesis.

1996 ◽  
Vol 70 (8) ◽  
pp. 4948-4952 ◽  
Author(s):  
J Zoll ◽  
J M Galama ◽  
F J van Kuppeveld ◽  
W J Melchers
Keyword(s):  
Protein Synthesis ◽  
Host Cell ◽  
Cell Protein ◽  
Host Cell Protein
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