Process of protein transport by the type III secretion system

被引:318
作者
Ghosh, P [1 ]
机构
[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
关键词
D O I
10.1128/MMBR.68.4.771-795.2004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The type HI secretion system (TTSS) of gram-negative bacteria is responsible for delivering bacterial proteins, termed effectors, from the bacterial cytosol directly into the interior of host cells. The TTSS is expressed predominantly by pathogenic bacteria and is usually used to introduce deleterious effectors into host cells. While biochemical activities of effectors vary widely, the TTSS apparatus used to deliver these effectors is conserved and shows functional complementarity for secretion and translocation. This review focuses on proteins that constitute the TTSS apparatus and on mechanisms that guide effectors to the TTSS apparatus for transport. The TTSS apparatus includes predicted integral inner membrane proteins that are conserved widely across TTSSs and in the basal body of the bacterial flagellum. It also includes proteins that are specific to the TTSS and contribute to ring-like structures in the inner membrane and includes secretin family members that form ring-like structures in the outer membrane. Most prominently situated on these coaxial, membrane-embedded rings is a needle-like or pilus-like structure that is implicated as a conduit for effector translocation into host cells. A short region of mRNA sequence or protein sequence in effectors acts as a signal sequence, directing proteins for transport through the TTSS. Additionally, a number of effectors require the action of specific TTSS chaperones for efficient and physiologically meaningful translocation into host cells. Numerous models explaining how effectors are transported into host cells have been proposed, but understanding of this process is incomplete and this topic remains an active area of inquiry.
引用
收藏
页码:771 / +
页数:26
相关论文
共 257 条
[31]   Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica [J].
Cheng, LW ;
Anderson, DM ;
Schneewind, O .
MOLECULAR MICROBIOLOGY, 1997, 24 (04) :757-765
[32]   Yersinia enterocolitica type III secretion -: On the role of SycE in targeting YopE into HeLa cells [J].
Cheng, LW ;
Schneewind, O .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (31) :22102-22108
[33]   Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly [J].
Claret, L ;
Calder, SR ;
Higgins, M ;
Hughes, C .
MOLECULAR MICROBIOLOGY, 2003, 48 (05) :1349-1355
[34]   Helical structure of the needle of the type III secretion system of Shigella flexneri [J].
Cordes, FS ;
Komoriya, K ;
Larquet, E ;
Yang, SX ;
Egelman, EH ;
Blocker, A ;
Lea, SM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (19) :17103-17107
[35]   TRANSCRIPTION OF THE YOP REGULON FROM Y-ENTEROCOLITICA REQUIRES TRANS ACTING PYV AND CHROMOSOMAL GENES [J].
CORNELIS, G ;
VANOOTEGEM, JC ;
SLUITERS, C .
MICROBIAL PATHOGENESIS, 1987, 2 (05) :367-379
[36]   The Yersinia YSC-YOP 'type III' weaponry [J].
Cornelis, GR .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2002, 3 (10) :742-752
[37]   Assembly and function of type III secretory systems [J].
Cornelis, GR ;
Van Gijsegem, F .
ANNUAL REVIEW OF MICROBIOLOGY, 2000, 54 :735-774
[38]   The virulence plasmid of Yersinia, an antihost genome [J].
Cornelis, GR ;
Boland, A ;
Boyd, AP ;
Geuijen, C ;
Iriarte, M ;
Neyt, C ;
Sory, MP ;
Stainier, I .
MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 1998, 62 (04) :1315-+
[39]   The Yersinia deadly kiss [J].
Cornelis, GR .
JOURNAL OF BACTERIOLOGY, 1998, 180 (21) :5495-5504
[40]   Yersinia type III secretion:: send in the effectors [J].
Cornelis, GR .
JOURNAL OF CELL BIOLOGY, 2002, 158 (03) :401-408