The type III secretion injectisome, a complex nanomachine for intracellular 'toxin' delivery

被引：94

作者：

Cornelis, Guy R. ^{[1
]}

机构：

[1] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland

来源：

BIOLOGICAL CHEMISTRY | 2010年 / 391卷 / 07期

关键词：

microbial pathogenesis; protein secretion; virulence; Yersinia; FLAGELLAR HOOK-LENGTH; PROTON MOTIVE FORCE; YERSINIA-ENTEROCOLITICA; SALMONELLA-TYPHIMURIUM; NEEDLE COMPLEX; PROTEIN SECRETION; V-ANTIGEN; SUPRAMOLECULAR STRUCTURE; PSEUDOMONAS-AERUGINOSA; SUBSTRATE-SPECIFICITY;

D O I：

10.1515/BC.2010.079

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：

The type III secretion injectisome is a nanomachine that delivers bacterial proteins into the cytosol of eukaryotic target cells. It consists of a cylindrical basal structure spanning the two bacterial membranes and the peptidoglycan, connected to a hollow needle, eventually followed by a filament (animal pathogens) or to a long pilus (plant pathogens). Export employs a type III pathway. During assembly, all the protein subunits of external elements are sequentially exported by the basal structure itself, implying that the export apparatus can switch its substrate specificity over time. The length of the needle is controlled by a protein that it also secreted during assembly and presumably acts as a molecular ruler.

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页码：745 / 751

页数：7

相关论文

共 91 条

[71] Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure [J].

Sekiya, K ;

Ohishi, M ;

Ogino, T ;

Tamano, K ;

Sasakawa, C ;

Abe, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (20) :11638-11643

[72] YscU recognizes translocators as export substrates of the Yersinia injectisome [J].

Sorg, Isabel ;

Wagner, Stefanie ;

Amstutz, Marlise ;

Mueller, Shirley A. ;

Broz, Petr ;

Lussi, Yvonne ;

Engel, Andreas ;

Cornelis, Guy R. .

EMBO JOURNAL, 2007, 26 (12) :3015-3024

[73] The Chlamydia Type III Secretion System C-ring Engages a Chaperone-Effector Protein Complex [J].

Spaeth, Kris E. ;

Chen, Yi-Shan ;

Valdivia, Raphael H. .

PLOS PATHOGENS, 2009, 5 (09)

[74] A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system [J].

Spreter, Thomas ;

Yip, Calvin K. ;

Sanowar, Sarah ;

Andre, Ingemar ;

Kimbrough, Tyler G. ;

Vuckovic, Marija ;

Pfuetzner, Richard A. ;

Deng, Wanyin ;

Yu, Angel C. ;

Finlay, B. Brett ;

Baker, David ;

Miller, Samuel I. ;

Strynadka, Natalie C. J. .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2009, 16 (05) :468-476

[75] Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ [J].

Sukhan, A ;

Kubori, T ;

Galán, JE .

JOURNAL OF BACTERIOLOGY, 2003, 185 (11) :3480-3483

[76] Genetic analysis of assembly of the Salmonella enterica serovar typhimurium type III secretion-associated needle complex [J].

Sukhan, A ;

Kubori, T ;

Wilson, J ;

Galán, JE .

JOURNAL OF BACTERIOLOGY, 2001, 183 (04) :1159-1167

[77] Supramolecular structure of the Shigella type III secretion machinery:: the needle part is changeable in length and essential for delivery of effectors [J].

Tamano, K ;

Aizawa, S ;

Katayama, E ;

Nonaka, T ;

Imajoh-Ohmi, S ;

Kuwae, A ;

Nagai, S ;

Sasakawa, C .

EMBO JOURNAL, 2000, 19 (15) :3876-3887

[78] The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar typhimurium [J].

Thomas, Dennis R. ;

Francis, Noreen R. ;

Xu, Chen ;

DeRosier, David J. .

JOURNAL OF BACTERIOLOGY, 2006, 188 (20) :7039-7048

[79] Type III secretion: More systems than you think [J].

Troisfontaines, P ;

Cornelis, GR .

PHYSIOLOGY, 2005, 20 :326-339

[80] DOMAIN-STRUCTURES OF THE MS RING COMPONENT PROTEIN (FLIF) OF THE FLAGELLAR BASAL BODY OF SALMONELLA-TYPHIMURIUM [J].

UENO, T ;

OOSAWA, K ;

AIZAWA, SI .

JOURNAL OF MOLECULAR BIOLOGY, 1994, 236 (02) :546-555

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