A Conserved Phenylalanine Residue of Autographa Californica Multiple Nucleopolyhedrovirus AC75 Protein Is Required for Occlusion Body Formation
Autor: | Xingang Chen, Jian Yang, Xiaoqin Yang, Chengfeng Lei, Xiulian Sun, Jia Hu |
---|---|
Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: | |
Zdroj: | Frontiers in Microbiology, Vol 12 (2021) |
Druh dokumentu: | article |
ISSN: | 1664-302X 38512653 |
DOI: | 10.3389/fmicb.2021.663506 |
Popis: | Autographa californica multiple nucleopolyhedrovirus (AcMNPV) orf75 (ac75) is a highly conserved gene that is essential for AcMNPV propagation. However, the key domains or residues of the AC75 protein that play a role in viral propagation have not been identified. In this study, sequence alignment revealed that residues Phe-54 and Gln-81 of AC75 were highly conserved among alphabaculoviruses and betabaculoviurses. Thus, Phe-54 and Gln-81 AC75 mutation bacmids were constructed. We found that Gln-81 was not required for viral propagation, whereas mutating Phe-54 reduced budded virus production by 10-fold and impaired occlusion body formation when compared with that of the wild-type AcMNPV. Electron microscopy observations showed that the Phe-54 mutation affected polyhedrin assembly and also occlusion-derived virus embedding, whereas western blot analysis revealed that mutating Phe-54 reduced the amount of AC75 but did not affect the localization of AC75 in infected cells. A protein stability assay showed that the Phe-54 mutation affected AC75 stability. Taken together, Phe-54 was identified as an important residue of AC75, and ac75 is a pivotal gene in budding virus production and occlusion body formation. |
Databáze: | Directory of Open Access Journals |
Externí odkaz: |