Protein secretion systems and adhesins: The molecular armory of Gram-negative pathogens

被引:209
作者
Gerlach, Roman G. [1 ]
Hensel, Michael [1 ]
机构
[1] Univ Klinikum Erlangen, Inst Klin Mikrobiol Immunol & Hyg, D-91054 Erlangen, Germany
关键词
bacterial protein secretion; fimbrial adhesins; non-fimbrial adhesins; Gram-negative pathogen; cell envelope;
D O I
10.1016/j.ijmm.2007.03.017
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Protein secretion is a basic cellular function found in organisms of all kingdoms of life. Gram-negative bacteria have evolved a remarkable number of pathways for the transport of proteins across the cell envelope. The secretion systems fulfill general cellular functions but are also essential for pathogenic bacteria during the interaction with eukaryotic host cells. Secretion systems range from relatively simple structures such as type I secretion systems composed of three subunits that only secrete one substrate protein to complex machines such as type III and IV secretion systems composed of more than 20 subunits that can translocate large sets of effector proteins into eukaryotic target cells. In this review, the main structural and functional features of secretion systems are described. One subgroup of substrate proteins of secretion systems are protein adhesins. Despite the conserved function in binding to host cell ligands or to abiotic surfaces, the assembly of the various bacterial adhesins is highly divergent. Here we give an overview on the recent understanding of the assembly of fimbrial and non-fimbrial adhesins and the role of type 1, 111 and V secretion systems and specialized branches of the general secretion pathway in their biogenesis. (c) 2007 Elsevier GmbH. All rights reserved.
引用
收藏
页码:401 / 415
页数:15
相关论文
共 127 条
[1]   Chaperone release and unfolding of substrates in type III secretion [J].
Akeda, Y ;
Galán, JE .
NATURE, 2005, 437 (7060) :911-915
[2]   Type IV secretion systems and their effectors in bacterial pathogenesis [J].
Backert, S ;
Meyer, TF .
CURRENT OPINION IN MICROBIOLOGY, 2006, 9 (02) :207-217
[3]   Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli [J].
Batchelor, M ;
Prasannan, S ;
Daniell, S ;
Reece, S ;
Connerton, I ;
Bloomberg, G ;
Dougan, G ;
Frankel, G ;
Matthews, S .
EMBO JOURNAL, 2000, 19 (11) :2452-2464
[4]   3-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS-AERUGINOSA - A 2-DOMAIN PROTEIN WITH A CALCIUM-BINDING PARALLEL-BETA ROLL MOTIF [J].
BAUMANN, U ;
WU, S ;
FLAHERTY, KM ;
MCKAY, DB .
EMBO JOURNAL, 1993, 12 (09) :3357-3364
[5]  
Baumler AJ, 1996, INFECT IMMUN, V64, P1862
[6]   Genome update:: prediction of secreted proteins in 225 bacterial proteomes [J].
Bendtsen, JD ;
Binnewies, TT ;
Hallin, PF ;
Sicheritz-Pontén, T ;
Ussery, DW .
MICROBIOLOGY-SGM, 2005, 151 :1725-1727
[7]  
BenNasr A, 1996, MOL MICROBIOL, V20, P927
[8]   Differential recognition of members of the carcinoembryonic antigen family by Afa/Dr adhesins of diffusely adhering Escherichia coli (Afa/Dr DAEC) [J].
Berger, CN ;
Billker, O ;
Meyer, TF ;
Servin, AL ;
Kansau, I .
MOLECULAR MICROBIOLOGY, 2004, 52 (04) :963-983
[9]   MOLECULAR CHARACTERIZATION OF A FIMBRIAL ADHESIN, F1845, MEDIATING DIFFUSE ADHERENCE OF DIARRHEA-ASSOCIATED ESCHERICHIA-COLI TO HEP-2 CELLS [J].
BILGE, SS ;
CLAUSEN, CR ;
LAU, W ;
MOSELEY, SL .
JOURNAL OF BACTERIOLOGY, 1989, 171 (08) :4281-4289
[10]   PROTEIN SECRETION BY HYBRID BACTERIAL ABC-TRANSPORTERS - SPECIFIC FUNCTIONS OF THE MEMBRANE ATPASE AND THE MEMBRANE-FUSION PROTEIN [J].
BINET, R ;
WANDERSMAN, C .
EMBO JOURNAL, 1995, 14 (10) :2298-2306