Proteome changes of lungs artificially infected with H-PRRSV and N-PRRSV by two-dimensional fluorescence difference gel electrophoresis.
BACKGROUND
Porcine reproductive and respiratory syndrome with PRRS virus (PRRSV) infection, which causes significant economic losses annually, is one of the most economically important diseases affecting swine industry worldwide. In 2006 and 2007, a large-scale outbreak of highly pathogenic porcine reproductive and respiratory syndrome (PRRS) happened in China and Vietnam. However little data is available on global host response to PRRSV infection at the protein level, and similar approaches looking at mRNA is problematic since mRNA levels do not necessarily predict protein levels. In order to improve the knowledge of host response and viral pathogenesis of highly virulent Chinese-type PRRSV (H-PRRSV) and Non-high-pathogenic North American-type PRRSV strains (N-PRRSV), we analyzed the protein expression changes of H-PRRSV and N-PRRSV infected lungs compared with those of uninfected negative control, and identified a series of proteins related to host response and viral pathogenesis.


RESULTS
According to differential proteomes of porcine lungs infected with H-PRRSV, N-PRRSV and uninfected negative control at different time points using two-dimensional fluorescence difference gel electrophoresis (2D-DIGE) and mass spectrometry identification, 45 differentially expressed proteins (DEPs) were identified. These proteins were mostly related to cytoskeleton, stress response and oxidation reduction or metabolism. In the protein interaction network constructed based on DEPs from lungs infected with H-PRRSV, HSPA8, ARHGAP29 and NDUFS1 belonged to the most central proteins, whereas DDAH2, HSPB1 and FLNA corresponded to the most central proteins in those of N-PRRSV infected.


CONCLUSIONS
Our study is the first attempt to provide the complex picture of pulmonary protein expression during H-PRRSV and N-PRRSV infection under the in vivo environment using 2D-DIGE technology and bioinformatics tools, provides large scale valuable information for better understanding host proteins-virus interactions of these two PRRSV strains.
Xiao
Shuqi
S
State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, China.
Wang
Qiwei
Q
Jia
Jianyu
J
Cong
Peiqing
P
Mo
Delin
D
Yu
Xiangchun
X
Qin
Limei
L
Li
Anning
A
Niu
Yuna
Y
Zhu
Kongju
K
Wang
Xiaoying
X
Liu
Xiaohong
X
Chen
Yaosheng
Y
D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D005260:Female; D005453:Fluorescence; D008168:Lung / Q000737:chemistry / Q000378:metabolism* / Q000821:virology; D008297:Male; D008969:Molecular Sequence Data; D019318:Porcine Reproductive and Respiratory Syndrome / Q000378:metabolism* / Q000821:virology; D019316:Porcine respiratory and reproductive syndrome virus / Q000145:classification / Q000472:pathogenicity / Q000502:physiology*; D020543:Proteome / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics; D013552:Swine; D014774:Virulence
D020543:Proteome