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Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1
- Source :
- Virology. 482
- Publication Year :
- 2014
-
Abstract
- Bacteriophage PRD1, which has been studied intensively at the structural and functional levels, still has some gene products with unknown functions and certain aspects of the PRD1 assembly process have remained unsolved. In this study, we demonstrate that the phage-encoded non-structural proteins P17 and P33, either individually or together, complement the defect in a temperature-sensitive GroES mutant of Escherichia coli for host growth and PRD1 propagation. Confocal microscopy of fluorescent fusion proteins revealed co-localisation between P33 and P17 as well as between P33 and the host chaperonin GroEL. A fluorescence recovery after photobleaching assay demonstrated that the diffusion of the P33 fluorescent fusion protein was substantially slower in E. coli than theoretically calculated, presumably resulting from intermolecular interactions. Our results indicate that P33 and P17 function in procapsid assembly, possibly in association with the host chaperonin complex GroEL/GroES.
- Subjects :
- assembly
chaperonin
viruses
Mutant
fluorescence recovery after photobleaching
Viral Nonstructural Proteins
medicine.disease_cause
Virus Replication
Chaperonin
Host-Parasite Interactions
Bacteriophage
bacteriophage
Virology
medicine
Escherichia coli
fluorescent protein
Bacteriophage PRD1
membrane virus
Microscopy, Confocal
biology
protein localisation
Virus Assembly
ta1182
Fluorescence recovery after photobleaching
GroES
Chaperonin 60
biology.organism_classification
Fusion protein
GroEL
3. Good health
Cell biology
Subjects
Details
- ISSN :
- 10960341
- Volume :
- 482
- Database :
- OpenAIRE
- Journal :
- Virology
- Accession number :
- edsair.doi.dedup.....893320eed07e8d95f378ca0b8f8b6fc2