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RNA-dependent RNA polymerase complex of Brome mosaic virus: analysis of the molecular structure with monoclonal antibodies
- Source :
- Journal of General Virology. 83:2879-2890
- Publication Year :
- 2002
- Publisher :
- Microbiology Society, 2002.
-
Abstract
- Viral RNA-dependent RNA polymerase (RdRp) plays crucial roles in the genomic replication and subgenomic transcription of Brome mosaic virus (BMV), a positive-stranded RNA plant virus. BMV RdRp is a complex of virus-encoded 1a and 2a proteins and some cellular factors, and associates with the endoplasmic reticulum at an infection-specific structure in the cytoplasm of host cells. In this study, we investigate the gross structure of the active BMV RdRp complex using monoclonal antibodies raised against the 1a and 2a proteins. Immunoprecipitation experiments showed that the intermediate region between the N-terminal methyltransferase-like domain and the C-terminal helicase-like domain of 1a protein, and the N terminus region of 2a protein are exposed on the surface of the solubilized RdRp complex. Inhibition assays for membrane-bound RdRp suggested that the intermediate region between the methyltransferase-like and the helicase-like domains of 1a protein is located at the border of the region buried within a membrane structure or with membrane-associated material.
- Subjects :
- Immunoprecipitation
viruses
Molecular Sequence Data
RNA-dependent RNA polymerase
Chemical Fractionation
Biology
Antibodies, Viral
Chromatography, DEAE-Cellulose
Mice
chemistry.chemical_compound
Brome mosaic virus
Transcription (biology)
Virology
Plant virus
RNA polymerase
Animals
Amino Acid Sequence
Subgenomic mRNA
Molecular Structure
Antibodies, Monoclonal
RNA
RNA-Dependent RNA Polymerase
biology.organism_classification
Bromovirus
Precipitin Tests
Molecular biology
chemistry
Ethanolamines
Epitopes, B-Lymphocyte
Epitope Mapping
Subjects
Details
- ISSN :
- 14652099 and 00221317
- Volume :
- 83
- Database :
- OpenAIRE
- Journal :
- Journal of General Virology
- Accession number :
- edsair.doi.dedup.....f72b58f79e7e21228708a769a7e7883b