Autographa californica Multiple Nucleopolyhedrovirus Ac34 Protein Retains Cellular Actin-Related Protein 2/3 Complex in the Nucleus by Subversion of CRM1-Dependent Nuclear Export

PLoS Pathogens

Kai Yang¹  Rongjuan Pei¹  Jizheng Chen¹  Jingfang Mu¹  Yangyang Hu¹  Chunchen Wu¹  Monique M. van Oers¹  Han Zhao¹  Xinwen Chen¹  Yuan Zhou¹  Yongli Zhang²  Xue Hu²  Yun Wang²  He Zhao² 

[1]State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China

[2]University of Chinese Academy of Sciences, Beijing, China

关键词: Actin polymerization;    Fluorescence microscopy;    Cytoplasm;    Actins;    Immunofluorescence microscopy;    Densitometry;    Nucleocapsids;    Viral replication;   

DOI  :  10.1371/journal.ppat.1005994

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

Actin, nucleation-promoting factors (NPFs), and the actin-related protein 2/3 complex (Arp2/3) are key elements of the cellular actin polymerization machinery. With nuclear actin polymerization implicated in ever-expanding biological processes and the discovery of the nuclear import mechanisms of actin and NPFs, determining Arp2/3 nucleo-cytoplasmic shuttling mechanism is important for understanding the function of nuclear actin. A unique feature of alphabaculovirus infection of insect cells is the robust nuclear accumulation of Arp2/3, which induces actin polymerization in the nucleus to assist in virus replication. We found that Ac34, a viral late gene product encoded by the alphabaculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV), is involved in Arp2/3 nuclear accumulation during virus infection. Further assays revealed that the subcellular distribution of Arp2/3 under steady-state conditions is controlled by chromosomal maintenance 1 (CRM1)-dependent nuclear export. Upon AcMNPV infection, Ac34 inhibits CRM1 pathway and leads to Arp2/3 retention in the nucleus.

【 授权许可】

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