Abstract
Cells infected with poliovirus express a virally encoded polyprotein which undergoes self-mediated cleavage into structural and nonstructural viral proteins. Most of these cleavages are catalyzed by the 3C proteolytic domain of the polyprotein. Polyprotein synthesized in vitro from an RNA template containing a three-nucleotide insertion in 3C underwent proteolytic processing at all but one of the 3C-dependent cleavage sites. When transfected into HeLa cells, this RNA template displayed a lethal phenotype. We report here the isolation of two pseudorevertant progeny strains with restored protein-processing phenotypes, one of which appears to have arisen by transduction of a stretch of nucleotides from human 28S rRNA.
MeSH Terms
Amino Acid Sequence
Base Sequence
HeLa Cells
Humans
Methionine/metabolism
Models, Genetic
Molecular Sequence Data
Mutagenesis, Site-Directed
Phenotype
Poliovirus/genetics,metabolism
Protein Biosynthesis
RNA, Ribosomal, 28S/biosynthesis
RNA, Viral/metabolism
Ribosomes/metabolism
Templates, Genetic
Transduction, Genetic
Transfection
Viral Proteins/biosynthesis
Chemicals
RNA, Ribosomal, 28S
RNA, Viral
Viral Proteins
Methionine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Charini W A
Department of Microbiology and Molecular Genetics, College of Medicine, University of California, Irvine 92717.
Todd S
Gutman G A
Semler B L
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