Expression of potyvirus coat protein in Escherichia coli and yeast and its assembly into virus-like particles

CSIRO, Division of Biomolecular Engineering, Parkville Laboratory, 343 Royal Parade, Parkville 3052, Victoria, Australia When the full-length coat protein (CP) of the potyvirus, Johnsongrass mosaic virus (JGMV), was expressed in Escherichia coli or yeast, it assembled to form potyvirus-like particle...

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Published inJournal of general virology Vol. 72; no. 7; pp. 1543 - 1550
Main Authors Jagadish, Mittur N, Ward, Colin W, Gough, Keith H, Tulloch, Peter A, Whittaker, Loyce A, Shukla, Dharma D
Format Journal Article
LanguageEnglish
Published Reading Soc General Microbiol 01.07.1991
Society for General Microbiology
Subjects
Amino Acid Sequence
Base Sequence
Biological and medical sciences
Capsid - biosynthesis
Capsid - genetics
Capsid - ultrastructure
Centrifugation, Density Gradient
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation, Viral
Genetic Vectors
Immunoblotting
Microbiology
Microscopy, Electron
Molecular Sequence Data
Morphology, structure, chemical composition, physicochemical properties
Mosaic Viruses - genetics
Mutagenesis, Site-Directed
Oligonucleotides - chemistry
Oligonucleotides - genetics
Plasmids
Protein Conformation
Saccharomyces cerevisiae - genetics
Virology
Plant pathogen
Escherichia coli
Virus like particle
Site directed mutagenesis
Gene expression
Electron microscopy
Fungi
Virus
Proteins
Molecular assembly
Morphology
Immunoblotting assay
Bacteria
Ascomycetes
Potyvirus
Capsid
Saccharomyces cerevisiae
Enterobacteriaceae
Thallophyta
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Summary:CSIRO, Division of Biomolecular Engineering, Parkville Laboratory, 343 Royal Parade, Parkville 3052, Victoria, Australia When the full-length coat protein (CP) of the potyvirus, Johnsongrass mosaic virus (JGMV), was expressed in Escherichia coli or yeast, it assembled to form potyvirus-like particles. The particles were heterogeneous in length with a stacked-ring appearance and resembled JGMV particles in their flexuous morphology and width. This cell-free assembly system should permit analysis of the mechanisms of particle assembly and genome encapsidation. Two mutant forms of CP produced by site-directed mutagenesis failed to assemble into virus-like particles. Received 14 December 1990; accepted 29 March 1991.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-72-7-1543