|Title||The cysteine-rich region of a baculovirus VP91 protein contributes to the morphogenesis of occlusion bodies|
|Author(s)||Zhou, Fengqiao; Kuang, Wenhua; Wang, Xi; Hou, Dianhai; Huang, Huachao; Sun, Xiulian; Deng, Fei; Wang, Hualin; Oers, Monqiue M. van; Wang, Manli; Hu, Zhihong|
|Source||Virology 535 (2019). - ISSN 0042-6822 - p. 144 - 153.|
Laboratory of Virology
|Publication type||Refereed Article in a scientific journal|
|Keyword(s)||Cysteine-rich region - Disulfide bond - HA76 - Occlusion body (OB) - Oral infection - P33 - Per os infectivity factor (PIF) - PIF8 - Polyhedra - VP91|
The baculovirus core gene vp91 has been reported to be essential for nucleocapsid assembly and oral infection. Here, we studied the function of vp91 by analyzing its homologue, ha76, in Helicoverpa armigera nucleopolyhedrovirus (HearNPV). HA76 was expressed at the late stage of HearNPV infection; deletion of ha76 showed that the gene is required for budded virus production. A series of recombinants with truncated ha76 was constructed and analyzed in vitro and in vivo. The results showed that the region encoding the C-terminus of HA76 was essential for nucleocapsid assembly, whereas the N-terminal cysteine-rich region was responsible for oral infection. Electron microscope analyses further showed that the cysteine-rich region contributed to morphogenesis of occlusion bodies (OBs), with amino acids 136–223 of HA76 being critical for this function. The results revealed a novel function of VP91 and suggested that the impact on OB morphogenesis is partially related to oral infectivity.