Document Detail

Cleavage of viral precursor proteins in vivo and in vitro.
MedLine Citation:
PMID:  4343549     Owner:  NLM     Status:  MEDLINE    
The use of protease inhibitors causes the accumulation of very large polypeptides (polyprotein) in tissue culture cells infected with either poliovirus or echovirus 12. The effectiveness of the inhibitor varies, depending on the cell line chosen. In infected monkey kidney cells, polyprotein is not cleaved when a chymotrypsin inhibitor is added, but in infected HeLa cells a trypsin inhibitor is most effective. Therefore, at least a part of the proteolytic activity is supplied by the host cell. Extracted viral polyprotein can be cleaved in vitro by trypsin or chymotrypsin. As estimated by migration in sodium dodecyl sulfate gels and antigenicity, chymotrypsin cleavage of the poliovirus polyprotein yields fragments which are similar to the in vivo product. The polyprotein is not in soluble form but is attached to a fast-sedimenting, membrane-bound structure. Proteolytic activities in cell extracts were assayed using polyprotein as substrate, and infected and uninfected extracts produced qualitatively dissimilar cleavages.
B D Korant
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of virology     Volume:  10     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  1972 Oct 
Date Detail:
Created Date:  1973-01-09     Completed Date:  1973-01-09     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  751-9     Citation Subset:  IM    
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MeSH Terms
Cell Line
Cell-Free System
Cells, Cultured
Chymotrypsin / antagonists & inhibitors,  pharmacology
Electrophoresis, Polyacrylamide Gel
Enterovirus B, Human / growth & development,  metabolism*
Hela Cells / metabolism
Ketones / pharmacology
Molecular Weight
Peptides / metabolism
Poliovirus / growth & development,  metabolism*
Precipitin Tests
Trypsin / pharmacology
Trypsin Inhibitors / pharmacology
Viral Proteins / biosynthesis,  metabolism*
Reg. No./Substance:
0/Ketones; 0/Peptides; 0/Trypsin Inhibitors; 0/Viral Proteins; 10028-17-8/Tritium; EC; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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