Expression of potyvirus coat protein in Escherichia coli and yeast and its assembly into virus-like particles.
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.
Jagadish
M N
MN
CSIRO, Division of Biomolecular Engineering, Parkville Laboratory, Victoria, Australia.
Ward
C W
CW
Gough
K H
KH
Tulloch
P A
PA
Whittaker
L A
LA
Shukla
D D
DD
D000595:Amino Acid Sequence; D001483:Base Sequence; D002213:Capsid / Q000096:biosynthesis / Q000235:genetics* / Q000648:ultrastructure; D002499:Centrifugation, Density Gradient; D004926:Escherichia coli / Q000235:genetics*; D015967:Gene Expression Regulation, Viral; D005822:Genetic Vectors; D015151:Immunoblotting; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009029:Mosaic Viruses / Q000235:genetics*; D016297:Mutagenesis, Site-Directed; D009841:Oligonucleotides / Q000737:chemistry / Q000235:genetics; D010957:Plasmids; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000235:genetics*
D009841:Oligonucleotides