Abstract
Chinese sacbrood virus (CSBV) is the major cause and lead to the collapse of Apis cerana colonies. VP1, the structural protein of CSBV, shows the highest variation in the amino acid sequences among proteins from different CSBV strains as well as exhibits excellent immunogenicity. However, its function with host protein still remains unclear. To clarify its function with host protein, we screened out host cellular proteins that interact with VP1 using the membrane protein yeast two-hybrid system. In addition, we verified interactions between heat shock protein 70 cognate 5 (Hsp70-c5) and VP1 using glutathione S-transferase (GST) pull-down and co-immunoprecipitation assays. VP1 and Hsp70-c5 were colocalized in the cytoplasm and nucleus. Using western blot and real-time polymerase chain reaction (PCR), Hsp70-c5 expression in CSBV-infected larvae was upregulated compared with that in healthy larvae. We observed that when we silenced Hsp70-c5, VP1 expression was significantly downregulated. These results demonstrate that Hsp70-c5 is involved in at least one stage(s) of the viral life cycle.
Highlights
Apis mellifera (Am) and Apis cerana (Ac) are major honey bee species in the global beekeeping industry (Zhang et al, 2014)
To identify cellular factors that potentially interact with Chinese sacbrood virus (CSBV) VP1, we needed to construct and evaluate a cDNA library
CSBV is the pathogen that majorly infects A. cerana, resulting in severe and lethal infections in colonies and eventual losses of entire colonies (Feng et al, 2013)
Summary
Apis mellifera (Am) and Apis cerana (Ac) are major honey bee species in the global beekeeping industry (Zhang et al, 2014). They are heavily infected by different vital viruses (Chen et al, 2004). Chinese sacbrood virus (CSBV) is the most serious threat to bee health and has caused wide spread concern among beekeepers and researchers (Sun et al, 2018). In 2008, epidemic outbreaks of CSD caused the death of individual bees and decimated entire bee colonies in Liaoning Province (Mingxiao et al, 2011)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.