Cloning and functional research of Arp2/3-P40/ARPC1 subunit of Sf9 cells.
- Author:
Shi-Li HAN
1
;
Jing-Fang MU
;
Yong-Li ZHANG
;
Xin-Wen CHEN
;
Yun WANG
;
Lu-Lin LI
Author Information
1. Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Science, Central China Normal University, Wuhan 430079, China. shanddonghanshili@126.com
- Publication Type:Journal Article
- MeSH:
Actin-Related Protein 2-3 Complex;
chemistry;
genetics;
metabolism;
Amino Acid Sequence;
Animals;
Capsid Proteins;
genetics;
metabolism;
Cell Line;
Cloning, Molecular;
Humans;
Insect Proteins;
chemistry;
genetics;
metabolism;
Molecular Sequence Data;
Nucleopolyhedrovirus;
genetics;
metabolism;
Phylogeny;
Protein Binding;
Sequence Alignment;
Sf9 Cells;
Spodoptera;
chemistry;
genetics;
metabolism;
virology
- From:
Chinese Journal of Virology
2012;28(6):601-608
- CountryChina
- Language:Chinese
-
Abstract:
The baculovirus-induced actin polymerization is mainly associated with the virus nucleocapsid protein P78/83, which is homologous with WASP proteins that can activate Arp2/3 complex and induce the actin polymerization. In order to explore the role of Arp2/3 complex in the baculovirus replication, the P40 subunit of Arp2/3 complex from Sf9 (Spodoptera frugiperda 9) cell line was cloned and characterized. Immunofluorescent microscopy assay indicated that P40 was recruited to the inner-side of nuclear membrane during virus infection, which was in accordance with nuclear F-actin distribution in virus-infected cells as documented in our previous research, suggesting P40 could be used to track Arp2/3 complex subcellular distribution changes during virus infection. In addition, co-immunoprecipitation assay demonstrated that P40 interacted with P78/83 only in virus-infected cells, suggesting that actin polymerization induced by P78/83-Arp2/3 complex during baculovirus infection was regulated by some unidentified virus factors.
