Profiling of cellular proteins in porcine reproductive and respiratory syndrome virus virions by proteomics analysis
文献类型： 外文期刊
作者： Zhang, Chengwen 1 ; Xue, Chunyi 1 ; Li, Yan 1 ; Kong, Qingming 1 ; Ren, Xiangpeng 1 ; Li, Xiaoming 1 ; Shu, Dingming 2 ;
作者机构： 1.Sun Yat Sen Univ, Sch Life Sci, State Key Lab Biocontrol, Guangzhou 510006, Guangdong, Peoples R China
2.Guangdong Acad Agr Sci, Inst Anim Sci, State Key Lab Livestock & Poultry Breeding, Guangzhou 510640, Peoples R China
3.S China Agr Univ, Coll Anim Sci, Guangzhou 510642, Guangdong, Peoples R China
期刊名称：VIROLOGY JOURNAL （ 影响因子：4.099； 五年影响因子：3.719 ）
ISSN： 1743-422X
年卷期： 2010 年 7 卷
页码：
收录情况： SCI
摘要： Background: Porcine reproductive and respiratory syndrome virus ( PRRSV) is an enveloped virus, bearing severe economic consequences to the swine industry worldwide. Previous studies on enveloped viruses have shown that many incorporated cellular proteins associated with the virion's membranes that might play important roles in viral infectivity. In this study, we sought to proteomically profile the cellular proteins incorporated into or associated with the virions of a highly virulent PRRSV strain GDBY1, and to provide foundation for further investigations on the roles of incorporated/associated cellular proteins on PRRSV's infectivity. Results: In our experiment, sixty one cellular proteins were identified in highly purified PRRSV virions by two-dimensional gel electrophoresis coupled with mass spectrometric approaches. The identified cellular proteins could be grouped into eight functional categories including cytoskeletal proteins, chaperones, macromolecular biosynthesis proteins, metabolism-associated proteins, calcium-dependent membrane-binding proteins and other functional proteins. Among the identified proteins, four have not yet been reported in other studied envelope viruses, namely, guanine nucleotide-binding proteins, tyrosine 3-monooxygenase/tryptophan 5-monooxygenase, peroxiredoxin 1 and galectin-1 protein. The presence of five selected cellular proteins (i.e., beta-actin, Tubulin, Annexin A2, heat shock protein Hsp27, and calcium binding proteins S100) in the highly purified PRRSV virions was validated by Western blot and immunogold labeling assays. Conclusions: Taken together, the present study has demonstrated the incorporation of cellular proteins in PRRSV virions, which provides valuable information for the further investigations for the effects of individual cellular proteins on the viral replication, assembly, and pathogenesis.
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