Porcine reproductive and respiratory syndrome virus induces autophagy to promote virus replication

An increasing number of studies demonstrate that autophagy, an intrinsic mechanism that can degrade cytoplasmic components, is involved in the infection processes of a variety of pathogens. It can be hijacked by various viruses to facilitate their replication. In this study, we found that PRRSV infe...

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Bibliographic Details
Published in:Autophagy 2012-10, Vol.8 (10), p.1434-1447
Main Authors: Sun, Ming-Xia, Huang, Li, Wang, Rui, Yu, Ya-Ling, Li, Chen, Li, Peng-Peng, Hu, Xiao-Chun, Hao, Hong-Ping, Ishag, Hassan A., Mao, Xiang
Format: Article
Language:English
Subjects:
Adenine - analogs & derivatives
Adenine - pharmacology
Animals
autophagosomes
autophagy
Autophagy - drug effects
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cell Line
Cell Survival - drug effects
Cycle
Endocytosis - drug effects
fusion
Gene Knockdown Techniques
Landes
lysosomes
Lysosomes - drug effects
Lysosomes - metabolism
Lysosomes - ultrastructure
Membrane Fusion - drug effects
Microtubule-Associated Proteins - metabolism
Organogenesis
Phagosomes - ultrastructure
Phagosomes - virology
Porcine Reproductive and Respiratory Syndrome - pathology
Porcine Reproductive and Respiratory Syndrome - virology
porcine reproductive and respiratory syndrome virus
Porcine respiratory and reproductive syndrome virus - drug effects
Porcine respiratory and reproductive syndrome virus - physiology
Porcine respiratory and reproductive syndrome virus - ultrastructure
Proteins
replication
RNA Interference - drug effects
Sirolimus - pharmacology
Swine - virology
Viral Nonstructural Proteins - metabolism
Virus Replication - drug effects
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Summary:An increasing number of studies demonstrate that autophagy, an intrinsic mechanism that can degrade cytoplasmic components, is involved in the infection processes of a variety of pathogens. It can be hijacked by various viruses to facilitate their replication. In this study, we found that PRRSV infection significantly increases the number of double- or single-membrane vesicles in the cytoplasm of host cells in ultrastructural analysis. Our results showed the LC3-I was converted into LC3-II after virus infection, suggesting the autophagy machinery was activated. We further used pharmacological agents and shRNAs to confirm that autophagy promoted the replication of PRRSV in host cells. Confocal microscopy analysis showed that PRRSV inhibited the fusion between autophagosomes and lysosomes, suggesting that PRRSV induced incomplete autophagy. This suppression caused the accumulation of autophagosomes which may serve as replication site to enhance PRRSV replication. It has been shown that NSP2 and NSP3 of arterivirus are two components of virus replication complex. We also found in our studies that NSP2 colocalized with LC3 in MARC-145 cells by performing confocal microscopy analysis and continuous density gradient centrifugation. Our studies presented here indicated that autophagy was activated during PRRSV infection and enhanced PRRSV replication in host cells by preventing autophagosome and lysosome fusion.
ISSN:1554-8627
1554-8635
DOI:10.4161/auto.21159