Subversion of Macrophage Functions by Bacterial Protein Toxins and Effectors

被引:8
作者
Wan, Muyang
Zhou, Yan [1 ]
Zhu, Yongqun [1 ]
机构
[1] Zhejiang Univ, Life Sci Inst, Hangzhou, Zhejiang, Peoples R China
基金
中国国家自然科学基金;
关键词
NF-KAPPA-B; SMALL GTPASE RAB1; LEGIONELLA-PNEUMOPHILA; MYCOBACTERIUM-TUBERCULOSIS; SHIGELLA-FLEXNERI; PHOSPHOTHREONINE LYASE; CELL-DEATH; INFLAMMATORY RESPONSE; TYROSINE-PHOSPHATASE; CONJUGATION SYSTEM;
D O I
10.21775/cimb.025.061
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Macrophages represent one of the first lines of host immune defences against the invasion of pathogenic bacteria. Many receptors, immune signalling pathways and cellular processes in macrophages, including Toll-like receptors, Nod-like receptors, phagocytosis, autophagy and programmed cell death, are involved in combating the infection of bacterial pathogens. For efficient colonization in the host, bacterial pathogens have evolved diverse mechanisms to interfere with macrophage functions to evade host defences. The major weapons utilized by bacterial pathogens are protein toxins and effectors secreted via specific bacterial secretion systems, including type I-VII secretion apparatuses. In recent years, great advances have been achieved in understanding how bacterial toxins and effectors subvert immune signalling and cellular processes of macrophages. In this review, we focus on the toxins and effectors that modulate the phagocytosis, intracellular immune signalling pathways, autophagy and programmed cell death processes of macrophages from the bacterium Legionella pneumophila, Shigella flexneri, Listeria monocytogenes, Salmonella spp., Yersinia spp., enteropathogenic E. coli and Mycobacterium tuberculosis.
引用
收藏
页码:61 / 79
页数:19
相关论文
共 93 条
[1]   ESX-1-induced apoptosis is involved in cell-to-cell spread of Mycobacterium tuberculosis [J].
Aguilo, J. I. ;
Alonso, H. ;
Uranga, S. ;
Marinova, D. ;
Arbues, A. ;
de Martino, A. ;
Anel, A. ;
Monzon, M. ;
Badiola, J. ;
Pardo, J. ;
Brosch, Roland ;
Martin, Carlos .
CELLULAR MICROBIOLOGY, 2013, 15 (12) :1994-2005
[2]   Macrophage Apoptosis Triggered by IpaD from Shigella flexneri [J].
Arizmendi, Olivia ;
Picking, William D. ;
Picking, Wendy L. .
INFECTION AND IMMUNITY, 2016, 84 (06) :1857-1865
[3]   A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKγ to dampen the host NF-κB-mediated inflammatory response [J].
Ashida, Hiroshi ;
Kim, Minsoo ;
Schmidt-Supprian, Marc ;
Ma, Averil ;
Ogawa, Michinaga ;
Sasakawa, Chihiro .
NATURE CELL BIOLOGY, 2010, 12 (01) :66-U164
[4]   Legionella pneumophila inhibits macrophage apoptosis by targeting pro-death members of the Bcl2 protein family [J].
Banga, Simran ;
Gao, Ping ;
Shen, Xihui ;
Fiscus, Valena ;
Zong, Wei-Xing ;
Chen, Lingling ;
Luo, Zhao-Qing .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (12) :5121-5126
[5]   Metalloprotease type III effectors that specifically cleave JNK and NF-κB [J].
Baruch, Kobi ;
Gur-Arie, Lihi ;
Nadler, Chen ;
Koby, Simi ;
Yerushalmi, Gal ;
Ben-Neriah, Yinon ;
Yogev, Orli ;
Shaulian, Eitan ;
Guttman, Chen ;
Zarivach, Raz ;
Rosenshine, Ilan .
EMBO JOURNAL, 2011, 30 (01) :221-231
[6]   Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles [J].
Birmingham, Cheryl L. ;
Canadien, Veronica ;
Kaniuk, Natalia A. ;
Steinberg, Benjamin E. ;
Higgins, Darren E. ;
Brumell, John H. .
NATURE, 2008, 451 (7176) :350-U13
[7]   Identification of p130(Cas) as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions [J].
Black, DS ;
Bliska, JB .
EMBO JOURNAL, 1997, 16 (10) :2730-2744
[8]   Molecular mechanisms involved in inflammasome activation [J].
Bryant, Clare ;
Fitzgerald, Katherine A. .
TRENDS IN CELL BIOLOGY, 2009, 19 (09) :455-464
[9]   Advances in Toll-like receptor biology: Modes of activation by diverse stimuli [J].
Bryant, Clare E. ;
Gay, Nick J. ;
Heymans, Stephane ;
Sacre, Sandra ;
Schaefer, Liliana ;
Midwood, Kim S. .
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2015, 50 (05) :359-379
[10]   STING is a direct innate immune sensor of cyclic di-GMP [J].
Burdette, Dara L. ;
Monroe, Kathryn M. ;
Sotelo-Troha, Katia ;
Iwig, Jeff S. ;
Eckert, Barbara ;
Hyodo, Mamoru ;
Hayakawa, Yoshihiro ;
Vance, Russell E. .
NATURE, 2011, 478 (7370) :515-U111