Effect of Poliovirus Double-Stranded RNA on Viral and Host-Cell Protein Synthesis

Celma, M L; Ehrenfeld, E

doi:10.1073/pnas.71.6.2440

Cited by 40 publications

(13 citation statements)

References 28 publications

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“…Coxsaekievirus-indueed inhibition of host protein synthesis is very similar to that in poliovirus-infeeted cells (8,28,27): the inhibition started soon after 2 hours PI; it was very rapid and virtually complete. Virus-specific protein synthesis began during the decline of host protein synthesis, increased during the ensuing period, and declined in late infection.…”

Section: Diseussionmentioning

confidence: 94%

Comparison of capsid polypeptides of group B coxsackieviruses and polypeptide synthesis in infected cells

Chatterjee

Tuchowski

1981

Archives of Virology

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Capsid polypeptides of all six types (B1-6) of group B coxsackieviruses were compared by high-resolution gel electrophoresis, and synthesis of protein and RNA in B4- or B5-infected HeLA cells was analyzed. Four polypeptides, VP1-4, were detected in each type. Another polypeptide, VP0, slightly larger than VP1, was also detected in trace amounts in some types. VP1-3 showed different but characteristic molecular weights (VP1, 34,500 to 37,000; VP2, 31,000 to 36,000; VP3, 26,000 to 32,500), and presented well-defined and reproducible differences in electrophoretic mobility. The molecular weight of VP4 ranged from 5,000 to 5,500. VP1 was largest in B2 and B4, smallest in B1, and of intermediate size in the other types. VP2 was largest in B4 and smallest in B2; VP3 was largest in B5 and B6 and smallest in B4. In B4- or B5-infected HeLa cells, host protein synthesis began to decline after 2 hours postinfection and was less than 20 percent of the control by 6 hours postinfection. Actinomycin D-resistant viral RNA synthesis started at about 2 hours postinfection, peaked by 5 hours, and then declined rapidly. Virus-specific protein synthesis began while host protein synthesis was declining, increased during the ensuing period, and declined in late infection. A number of virus-specific proteins with molecular weights from 23,500 to greater than 92,500 were detected in the host cytoplasm. At least three of these proteins were also present in the nucleus. The kinetics pf processing of virus-specific proteins were examined by pulse-chase experiments in B5-infected cells. The relative intensities of [35S]-methionine-labeled polypeptides suggest that a number of smaller, stable chains (MW 23,500 to 38,000) are generated by cleavage of a precursor polypeptide (MW 92,500 to 100,000).

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Section: Diseussionmentioning

confidence: 94%

Comparison of capsid polypeptides of group B coxsackieviruses and polypeptide synthesis in infected cells

Chatterjee

Tuchowski

1981

Archives of Virology

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“…[32P]pCp was from Amersham Corp., Arlington Heights, Ill. All other radionuclides were from New England Nuclear Corp., Boston, Mass. Cells and virus. Growth of HeLa S3 cells and purification of the Mahoney strain of poliovirus type 1 have been described (10).…”

Section: Methodsmentioning

confidence: 99%

Host factor-induced template modification during synthesis of poliovirus RNA in vitro

Hey¹,

Richards²,

Ehrenfeld³

1987

J Virol

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Poliovirus RNA polymerase, 3DPOI, transcribes poliovirus RNA in vitro in the presence of a host factor (HF) preparation from uninfected HeLa cells to yield heterogeneous-size product RNAs. The products include some molecules larger than the template that represent self-primed elongations of the template from a 3'-terminal hairpin. We showed that transcription proceeded through the formation of a modified RNA intermediate that was generated by nucleolytic cleavage of the template by HF in the absence of nucleoside triphosphates. Cleavage resulted in the loss of the original poly(A) 3' end and the generation of new, heterogeneous 3' ends that formed self-priming structures that could then be elongated by 3DPo or reverse transcriptase. The two stages of the reaction, (i) cleavage to yield self-priming templates and (ii) subsequent chain elongation to yield heterogeneous-size products up to nearly dimer length, could be separated. RNAs whose original 3' ends were chemically oxidized so as to prevent chain elongation showed no reduction in template activity after preincubation with HF. We conclude that an HF preparation that contains a low level of nuclease activity is sufficient to activate RNA templates for transcription by 3D""' to generate up to apparent dimer-length products. This reaction likely has little relevance to the mechanism of poliovirus RNA replication in vivo. It is likely that numerous other factors or activities, in addition to 3DP"', would also result in transcription of poliovirus RNA in vitro.

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“…(3) Bossart and Bienz (1981); Femandez-Munoz and Darnell (1976). (4) Celma and Ehrenfeld (1974). (5) h e a l and .…”

Section: A Cautionary Notesmentioning

confidence: 99%

Regulation of Protein Synthesis in Virus-Infected Animal Cells

Kozak

1986

Advances in Virus Research Volume 31

178

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Effect of Poliovirus Double-Stranded RNA on Viral and Host-Cell Protein Synthesis

Cited by 40 publications

References 28 publications

Comparison of capsid polypeptides of group B coxsackieviruses and polypeptide synthesis in infected cells

Comparison of capsid polypeptides of group B coxsackieviruses and polypeptide synthesis in infected cells

Host factor-induced template modification during synthesis of poliovirus RNA in vitro

Regulation of Protein Synthesis in Virus-Infected Animal Cells

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