Protein delivery into eukaryotic cells by type III secretion machines

被引:797
作者
Galan, Jorge E. [1 ]
Wolf-Watz, Hans
机构
[1] Yale Univ, Sch Med, Boyer Ctr Mol Med, Sect Microbial Pathogenesis, New Haven, CT 06536 USA
[2] Umea Univ, Dept Mol Biol, SE-90187 Umea, Sweden
关键词
D O I
10.1038/nature05272
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Bacteria that have sustained long-standing close associations with eukaryotic hosts have evolved specific adaptations to survive and replicate in this environment. Perhaps one of the most remarkable of those adaptations is the type III secretion system (T3SS) - a bacterial organelle that has specifically evolved to deliver bacterial proteins into eukaryotic cells. Although originally identified in a handful of pathogenic bacteria, T3SSs are encoded by a large number of bacterial species that are symbiotic or pathogenic for humans, other animals including insects or nematodes, and plants. The study of these systems is leading to unique insights into not only organelle assembly and protein secretion but also mechanisms of symbiosis and pathogenesis.
引用
收藏
页码:567 / 573
页数:7
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共 84 条
[11]   Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization [J].
Crago, AM ;
Koronakis, V .
MOLECULAR MICROBIOLOGY, 1998, 30 (01) :47-56
[12]   Polarity of enteropathogenic Escherichia coli EspA filament assembly and protein secretion [J].
Crepin, VF ;
Shaw, R ;
Abe, CM ;
Knutton, S ;
Frankel, G .
JOURNAL OF BACTERIOLOGY, 2005, 187 (08) :2881-2889
[13]   Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ [J].
Crepin, VF ;
Prasannan, S ;
Shaw, RK ;
Wilson, RK ;
Creasey, E ;
Abe, CM ;
Knutton, S ;
Frankel, G ;
Matthews, S .
MOLECULAR MICROBIOLOGY, 2005, 55 (06) :1658-1670
[14]   The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG [J].
Daefler, S ;
Russel, M .
MOLECULAR MICROBIOLOGY, 1998, 28 (06) :1367-1380
[15]   The filamentous type III secretion translocon of enteropathogenic Escherichia coli [J].
Daniell, SJ ;
Takahashi, N ;
Wilson, R ;
Friedberg, D ;
Rosenshine, I ;
Booy, FP ;
Shaw, RK ;
Knutton, S ;
Frankel, G ;
Aizawa, S .
CELLULAR MICROBIOLOGY, 2001, 3 (12) :865-871
[16]   A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis [J].
Day, JB ;
Plano, GV .
MOLECULAR MICROBIOLOGY, 1998, 30 (04) :777-788
[17]   Induction of type III secretion in Shigella flexneri is associated with differential control of transcription of genes encoding secreted proteins [J].
Demers, B ;
Sansonetti, PJ ;
Parsot, C .
EMBO JOURNAL, 1998, 17 (10) :2894-2903
[18]   YscP and YscU regulate substrate specificity of the Yersinia type III secretion system [J].
Edqvist, PJ ;
Olsson, J ;
Lavander, M ;
Sundberg, L ;
Forsberg, Å ;
Wolf-Watz, H ;
Lloyd, SA .
JOURNAL OF BACTERIOLOGY, 2003, 185 (07) :2259-2266
[19]   The multitalented type III chaperones: all you can do with 15 kDa [J].
Feldman, MF ;
Cornelis, GR .
FEMS MICROBIOLOGY LETTERS, 2003, 219 (02) :151-158
[20]   Regulation of type III secretion systems [J].
Francis, MS ;
Wolf-Watz, H ;
Forsberg, Å .
CURRENT OPINION IN MICROBIOLOGY, 2002, 5 (02) :166-172