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In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA
- Source :
- Virology, vol 207, iss 2
- Publication Year :
- 1995
- Publisher :
- eScholarship, University of California, 1995.
-
Abstract
- The small spherical plant virus, cowpea chlorotic mottle virus (CCMV), provides an ideal system to examine spherical virus assembly. We have modified the CCMV in vitro assembly system to produce virions from coat protein expressed in Escherichia coli and viral RNA transcribed in vitro from full-length cDNAs. Examination of the in vitro-assembled particles with cryoelectron microscopy and image reconstruction techniques demonstrates that the particles are indistinguishable from plant purified particles at 2.5 nm resolution. Mutational analysis of the coat protein N- and C-terminal extensions demonstrate their respective roles in virus assembly. The N-terminus is required for assembly of RNA containing particles but not for the assembly of empty virions. The C-terminus is essential for coat protein dimer formation and particle assembly.
- Subjects :
- Models, Molecular
Transcription, Genetic
Protein Conformation
viruses
Image Processing
Gene Expression
medicine.disease_cause
Medical and Health Sciences
Protein structure
Computer-Assisted
Transcription (biology)
Models
Complementary
Image Processing, Computer-Assisted
2.2 Factors relating to the physical environment
Viral
Aetiology
Microscopy
biology
Plants
Biological Sciences
Bromovirus
Infection
Transcription
Biotechnology
DNA, Complementary
Molecular Sequence Data
Electron
Virus
Vaccine Related
Capsid
Genetic
Complementary DNA
Plant virus
Virology
medicine
Escherichia coli
DNA Primers
Cowpea chlorotic mottle virus
Base Sequence
Agricultural and Veterinary Sciences
RNA
Molecular
DNA
biology.organism_classification
Molecular biology
Microscopy, Electron
Emerging Infectious Diseases
DNA, Viral
Mutation
Subjects
Details
- Database :
- OpenAIRE
- Journal :
- Virology, vol 207, iss 2
- Accession number :
- edsair.doi.dedup.....d619ae760c61fa759333ae8684d1e78e