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Poliovirus Protease 3C (P3-7c) Does Not Cleave P220 of the Eucaryotic MRNA Cap-binding Protein Complex

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Journal J Virol
Date 1985 Aug 1
PMID 2991572
Citations 9
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Abstract

Infection of HeLa cells by poliovirus results in proteolysis of the large subunit (P220) of the cap-binding protein complex. This is believed to cause the rapid shut-off of host protein synthesis during poliovirus infection. In this communication we examined the possible involvement of poliovirus proteins 3C (a proteinase) and 2C in cleavage of P220. Using antisera against these two viral polypeptides, we were unable to inhibit proteolysis of P220 in an in vitro assay. These results indicate that viral proteins 3C and 2C are not directly involved in cleaving P220 and hence do not cause shut-off of cellular protein synthesis.

Citing Articles

Poliovirus proteinase 2A induces cleavage of eucaryotic initiation factor 4F polypeptide p220.

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PMID: 3039165 PMC: 255777. DOI: 10.1128/JVI.61.9.2711-2718.1987.


Restriction of translation of capped mRNA in vitro as a model for poliovirus-induced inhibition of host cell protein synthesis: relationship to p220 cleavage.

Lloyd R, Jense H, EHRENFELD E J Virol. 1987; 61(8):2480-8.

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Proteolysis of the p220 component of the cap-binding protein complex is not sufficient for complete inhibition of host cell protein synthesis after poliovirus infection.

Bonneau A, Sonenberg N J Virol. 1987; 61(4):986-91.

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Regulation of protein synthesis in virus-infected animal cells.

Kozak M Adv Virus Res. 1986; 31:229-92.

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Poliovirus mutant that does not selectively inhibit host cell protein synthesis.

Bernstein H, Sonenberg N, Baltimore D Mol Cell Biol. 1985; 5(11):2913-23.

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