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Groundnut Bud Necrosis Virus Encoded NSm Associates with Membranes via Its C-Terminal Domain
- Source :
- PLoS ONE, PLoS ONE, Vol 9, Iss 6, p e99370 (2014)
- Publication Year :
- 2014
- Publisher :
- PUBLIC LIBRARY SCIENCE, 2014.
-
Abstract
- Groundnut Bud Necrosis Virus (GBNV) is a tripartite ambisense RNA plant virus that belongs to serogroup IV of Tospovirus genus. Non-Structural protein-m (NSm), which functions as movement protein in tospoviruses, is encoded by the M RNA. In this communication, we demonstrate that despite the absence of any putative transmembrane domain, GBNV NSm associates with membranes when expressed in E. coli as well as in N. benthamiana. Incubation of refolded NSm with liposomes ranging in size from 200-250 nm resulted in changes in the secondary and tertiary structure of NSm. A similar behaviour was observed in the presence of anionic and zwitterionic detergents. Furthermore, the morphology of the liposomes was found to be modified in the presence of NSm. Deletion of coiled coil domain resulted in the inability of in planta expressed NSm to interact with membranes. Further, when the C-terminal coiled coil domain alone was expressed, it was found to be associated with membrane. These results demonstrate that NSm associates with membranes via the C-terminal coiled coil domain and such an association may be important for movement of viral RNA from cell to cell.
- Subjects :
- Genes, Viral
Plant Pathogens
lcsh:Medicine
Centrifugation
Plant Science
Biology
Microbiology
Biochemistry
Viral Proteins
Plant Microbiology
Tospovirus
Movement protein
lcsh:Science
Integral membrane protein
DNA Primers
Coiled coil
Microbiology & Cell Biology
Multidisciplinary
Base Sequence
C-terminus
lcsh:R
RNA
Biology and Life Sciences
Plant Pathology
biology.organism_classification
Molecular biology
Protein tertiary structure
Transmembrane domain
Liposomes
lcsh:Q
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 23813652
- Database :
- OpenAIRE
- Journal :
- IndraStra Global
- Accession number :
- edsair.doi.dedup.....f1d7615991c03e7dd43eb3c8722f973a