Effectors Targeting the Unfolded Protein Response during Intracellular Bacterial Infection

被引:23
作者
Alshareef, Manal H. [1 ,2 ,3 ]
Hartland, Elizabeth L. [1 ,2 ]
McCaffrey, Kathleen [1 ,2 ]
机构
[1] Hudson Inst Med Res, Ctr Innate Immun & Infect Dis, Clayton, Vic 3168, Australia
[2] Monash Univ, Dept Mol & Translat Sci, Clayton, Vic 3168, Australia
[3] Umm Al Qura Univ, Coll Pharm, Mecca 24230, Saudi Arabia
基金
英国医学研究理事会;
关键词
ER stress; UPR; bacteria; infection; secretion systems; effector proteins;
D O I
10.3390/microorganisms9040705
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The unfolded protein response (UPR) is a homeostatic response to endoplasmic reticulum (ER) stress within eukaryotic cells. The UPR initiates transcriptional and post-transcriptional programs to resolve ER stress; or, if ER stress is severe or prolonged, initiates apoptosis. ER stress is a common feature of bacterial infection although the role of the UPR in host defense is only beginning to be understood. While the UPR is important for host defense against pore-forming toxins produced by some bacteria, other bacterial effector proteins hijack the UPR through the activity of translocated effector proteins that facilitate intracellular survival and proliferation. UPR-mediated apoptosis can limit bacterial replication but also often contributes to tissue damage and disease. Here, we discuss the dual nature of the UPR during infection and the implications of UPR activation or inhibition for inflammation and immunity as illustrated by different bacterial pathogens.
引用
收藏
页数:12
相关论文
共 84 条
[41]   Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1α-mediated NF-κB activation and down-regulation of TRAF2 expression [J].
Hu, P ;
Han, Z ;
Couvillon, AD ;
Kaufman, RJ ;
Exton, JH .
MOLECULAR AND CELLULAR BIOLOGY, 2006, 26 (08) :3071-3084
[42]   The Legionella pneumophila replication vacuole: making a cosy niche inside host cells [J].
Isberg, Ralph R. ;
O'Connor, Tamara J. ;
Heidtman, Matthew .
NATURE REVIEWS MICROBIOLOGY, 2009, 7 (01) :12-24
[43]   Emerging functions of the unfolded protein response in immunity [J].
Janssens, Sophie ;
Pulendran, Bali ;
Lambrecht, Bart N. .
NATURE IMMUNOLOGY, 2014, 15 (10) :910-919
[44]   Calreticulin modulates the intracellular survival of mycobacteria by regulating ER-stress-mediated apoptosis [J].
Jo, Sung Hee ;
Choi, Ji-Ae ;
Lim, Yun-Ji ;
Lee, Junghwan ;
Cho, Soo-Na ;
Oh, Sung-Man ;
Go, Dam ;
Kim, Seon-Hwa ;
Song, Chang-Hwa .
ONCOTARGET, 2017, 8 (35) :58686-58698
[45]   NOD1/NOD2 signaling links ER stress with inflammation [J].
Keestra-Gounder, A. Marijke ;
Byndloss, Mariana X. ;
Seyffert, Nubia ;
Young, Briana M. ;
Chavez-Arroyo, Alfredo ;
Tsai, April Y. ;
Cevallos, Stephanie A. ;
Winter, Maria G. ;
Pham, Oanh H. ;
Tiffany, Connor R. ;
de Jong, Maarten F. ;
Kerrinnes, Tobias ;
Ravindran, Resmi ;
Luciw, Paul A. ;
McSorley, Stephen J. ;
Baumler, Andreas J. ;
Tsolis, Renee M. .
NATURE, 2016, 532 (7599) :394-397
[46]   The unfolded protein response signals through high-order assembly of Ire1 [J].
Korennykh, Alexei V. ;
Egea, Pascal F. ;
Korostelev, Andrei A. ;
Finer-Moore, Janet ;
Zhang, Chao ;
Shokat, Kevan M. ;
Stroud, Robert M. ;
Walter, Peter .
NATURE, 2009, 457 (7230) :687-U2
[47]   A molecular chaperone inducer protects neurons from ER stress [J].
Kudo, T. ;
Kanemoto, S. ;
Hara, H. ;
Morimoto, N. ;
Morihara, T. ;
Kimura, R. ;
Tabira, T. ;
Imaizumi, K. ;
Takeda, M. .
CELL DEATH AND DIFFERENTIATION, 2008, 15 (02) :364-375
[48]   Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells [J].
Lee, Sang-Yun ;
Lee, Moo-Seung ;
Cherla, Rama P. ;
Tesh, Vernon L. .
CELLULAR MICROBIOLOGY, 2008, 10 (03) :770-780
[49]   Endoplasmic Reticulum Stress Pathway-Mediated Apoptosis in Macrophages Contributes to the Survival of Mycobacterium tuberculosis [J].
Lim, Yun-Ji ;
Choi, Ji-Ae ;
Choi, Hong-Hee ;
Cho, Soo-Na ;
Kim, Hwa-Jung ;
Jo, Eun-Kyeong ;
Park, Jeong-Kyu ;
Song, Chang-Hwa .
PLOS ONE, 2011, 6 (12)
[50]   CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum [J].
Marciniak, SJ ;
Yun, CY ;
Oyadomari, S ;
Novoa, I ;
Zhang, YH ;
Jungreis, R ;
Nagata, K ;
Harding, HP ;
Ron, D .
GENES & DEVELOPMENT, 2004, 18 (24) :3066-3077