Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 536474
Title The group I alphabaculovirus-specific protein, AC5, is a novel component of the occlusion body but is not associated with ODVS or the PIF complex
Author(s) Wang, Xi; Chen, Cheng; Zhang, Nan; Li, Jiang; Deng, Fei; Wang, Hualin; Vlak, Just M.; Hu, Zhihong; Wang, Manli
Source Journal of General Virology 99 (2018)4. - ISSN 0022-1317 - p. 585 - 595.
DOI http://dx.doi.org/10.1099/jgv.0.001031
Department(s) FBR Post Harvest Technology
Laboratory of Virology
PE&RC
Publication type Refereed Article in a scientific journal
Publication year 2018
Keyword(s) Ac5 - Baculovirus - Function - Group I alphabaculovirus - Occlusion body - PIF complex
Abstract Autographa californica nucleopolyhedrovirus (AcMNPV) orf5 (ac5) is a group I alphabaculovirus-specific gene of unknown function, although the protein (AC5) was previously reported to be associated with the per os infectivity factor (PIF) complex. The purpose of this study was to study the dynamics of AC5 during AcMNPV infection and to verify whether it is indeed a component of the PIF complex. Transcription and expression analyses suggested that ac5 is a late viral gene. An ac5-deleted recombinant AcMNPV was generated by homologous recombination. A one-step growth curve assay indicated that ac5 was not required for budded virus (BV) production in Sf9 cells. Scanning electron microscopy and transmission electron microscopy demonstrated that the deletion of ac5 did not affect occlusion body (OB) morphology, and nor did it affect the insertion of occlusion-derived virus (ODV) into OBs. Partially denaturing SDS-PAGE and a co-immunoprecipitation assay clearly showed that AC5 was not a component of the PIF complex, while the deletion of ac5 did not affect the formation and presence of the PIF complex. Further analyses showed, however, that AC5 was an OB-specific protein, but it was not detected as a component of BVs or ODVs. Bioassay experiments showed that the oral infectivity of ac5-deleted AcMNPV to third instar Spodoptera exigua larvae was not significantly different from that of the ac5-repaired virus. In conclusion, AC5 is an intrinsic protein of OBs, instead of being a component of the PIF complex, and is not essential for either BV or ODV infection. AC5 is awaiting the assignment of another hitherto unknown function.
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