The Interaction between Nidovirales and Autophagy Components

被引:21
作者
Cong, Yingying [1 ]
Verlhac, Pauline [1 ]
Reggiori, Fulvio [1 ]
机构
[1] Univ Groningen, Univ Med Ctr Groningen, Dept Cell Biol, A Deusinglaan 1, NL-9713 AV Groningen, Netherlands
来源
VIRUSES-BASEL | 2017年 / 9卷 / 07期
基金
瑞士国家科学基金会;
关键词
coronavirus; arterivirus; mesonivirus; ronivirus; autophagosome; autophagic flux; infection; replication; egression; ENDOPLASMIC-RETICULUM STRESS; VIRUS INDUCES AUTOPHAGY; EQUINE ARTERITIS VIRUS; RESPIRATORY-SYNDROME; CORONAVIRUS REPLICATION; MEMBRANE-VESICLES; PRRSV INFECTION; ERAD REGULATORS; SPIKE PROTEIN; ATG PROTEINS;
D O I
10.3390/v9070182
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Autophagy is a conserved intracellular catabolic pathway that allows cells to maintain homeostasis through the degradation of deleterious components via specialized double-membrane vesicles called autophagosomes. During the past decades, it has been revealed that numerous pathogens, including viruses, usurp autophagy in order to promote their propagation. Nidovirales are an order of enveloped viruses with large single-stranded positive RNA genomes. Four virus families (Arterividae, Coronaviridae, Mesoniviridae, and Roniviridae) are part of this order, which comprises several human and animal pathogens of medical and veterinary importance. In host cells, Nidovirales induce membrane rearrangements including autophagosome formation. The relevance and putative mechanism of autophagy usurpation, however, remain largely elusive. Here, we review the current knowledge about the possible interplay between Nidovirales and autophagy.
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页数:14
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共 97 条
[1]  
Abdul-Rasool S., 2010, OPEN VIROL J, P4
[2]   Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum [J].
Axe, Elizabeth L. ;
Walker, Simon A. ;
Manifava, Maria ;
Chandra, Priya ;
Roderick, H. Llewelyn ;
Habermann, Anja ;
Griffiths, Gareth ;
Ktistakis, Nicholas T. .
JOURNAL OF CELL BIOLOGY, 2008, 182 (04) :685-701
[3]   ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER [J].
Bernasconi, Riccardo ;
Molinari, Maurizio .
CURRENT OPINION IN CELL BIOLOGY, 2011, 23 (02) :176-183
[4]   Hidden Behind Autophagy: The Unconventional Roles of ATG Proteins [J].
Bestebroer, Jovanka ;
V'kovski, Philip ;
Mauthe, Mario ;
Reggiori, Fulvio .
TRAFFIC, 2013, 14 (10) :1029-1041
[5]  
Bosch BJ, 2008, NIDOVIRUSES, P157
[6]   Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities [J].
Cali, Tito ;
Galli, Carmela ;
Olivari, Silvia ;
Molinari, Maurizio .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2008, 371 (03) :405-410
[7]   REVISION OF THE TAXONOMY OF THE CORONAVIRUS, TOROVIRUS AND ARTERIVIRUS GENERA [J].
CAVANAGH, D ;
BRIEN, DA ;
BRINTON, M ;
ENJUANES, L ;
HOLMES, KV ;
HORZINEK, MC ;
LAI, MMC ;
LAUDE, H ;
PLAGEMANN, PGW ;
SIDDELL, S ;
SPAAN, WJM ;
TAGUCHI, F ;
TALBOT, PJ .
ARCHIVES OF VIROLOGY, 1994, 135 (1-2) :227-237
[8]   Induction of autophagy enhances porcine reproductive and respiratory syndrome virus replication [J].
Chen, Quangang ;
Fang, Liurong ;
Wang, Dang ;
Wang, Shaohua ;
Li, Ping ;
Li, Mao ;
Luo, Rui ;
Chen, Huanchun ;
Xiao, Shaobo .
VIRUS RESEARCH, 2012, 163 (02) :650-655
[9]   Coronavirus membrane-associated papain-like proteases induce autophagy through interacting with Beclin1 to negatively regulate antiviral innate immunity [J].
Chen, Xiaojuan ;
Wang, Kai ;
Xing, Yaling ;
Tu, Jian ;
Yang, Xingxing ;
Zhao, Qian ;
Li, Kui ;
Chen, Zhongbin .
PROTEIN & CELL, 2014, 5 (12) :912-927
[10]   Coronavirus entry and release in polarized epithelial cells: a review [J].
Cong, Yingying ;
Ren, Xiaofeng .
REVIEWS IN MEDICAL VIROLOGY, 2014, 24 (05) :308-315