Bombyx mori nucleopolyhedrovirus ORF79 is a per os infectivity factor associated with the PIF complex
| Autor: | Qian He, Min-Hui Pan, Cheng Lu, Xue-Mei Chen, Hai-Qing Li, Ming-Ya Cao, Xiao Wenfu, Jun Zhang, Zhan-Qi Dong, Cai-xia Pan, La Wang |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Cancer Research
Nuclear Envelope viruses Protein combining Protein Sorting Signals medicine.disease_cause Immunofluorescence Virus Viral Envelope Proteins Bombyx mori Virology Protein Interaction Mapping Escherichia coli medicine Animals Infectivity Sequence Homology Amino Acid biology medicine.diagnostic_test fungi Virus Internalization Bombyx biology.organism_classification Molecular biology Nucleopolyhedroviruses Autographa californica Infectious Diseases Microscopy Fluorescence Protein Multimerization Homologous recombination Gene Deletion |
| Zdroj: | Virus Research. 184:62-70 |
| ISSN: | 0168-1702 |
| Popis: | Bombyx mori nucleopolyhedrovirus (BmNPV) ORF79 ( Bm79 ) encodes an occlusion-derived virus (ODV)-specific envelope protein, which is a homologue of the per os infectivity factor 4 (PIF4) of Autographa californica multiple nucleopolyhedrovirus (AcMNPV). To investigate the role of ORF79 in the BmNPV life cycle, a Bm79 knockout virus (vBm Bm79KO ) was constructed through homologous recombination in Escherichia coli. Viral DNA replication, budded virus (BV) production and polyhedra formation were unaffected by the absence of BM79. However, results of the larval bioassay demonstrated that the Bm79 deletion resulted in a complete loss of per os infection. Immunofluorescence analysis showed that BM79 localized at the innernuclear membrane of infected cells through its N-terminal sorting motif (SM). Further bimolecular fluorescence protein complementation and co-immunoprecipitation assays demonstrated the interaction of BM79 with PIF1, PIF2, PIF3 and ODV-E66. Thus, BM79 plays an important role in per os infection and is associated with the viral PIF complex of BmNPV. |
| Databáze: | OpenAIRE |
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