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

被引:210
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
[41]   Type IV pilin structures: Insights on shared architecture, fiber assembly, receptor binding and type II secretion [J].
Hansen, Johanna K. ;
Forest, Katrina T. .
JOURNAL OF MOLECULAR MICROBIOLOGY AND BIOTECHNOLOGY, 2006, 11 (3-5) :192-207
[42]   Identification of a domain in Yersinia virulence factor YadA that is crucial for extracellular matrix-specific cell adhesion and uptake [J].
Heise, T ;
Dersch, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (09) :3375-3380
[43]   Biofilm formation by Pseudomonas fluorescens WCS365:: a role for LapD [J].
Hinsa, Shannon M. ;
O'Toole, George A. .
MICROBIOLOGY-SGM, 2006, 152 :1375-1383
[44]   Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein [J].
Hinsa, SM ;
Espinosa-Urgel, M ;
Ramos, JL ;
O'Toole, GA .
MOLECULAR MICROBIOLOGY, 2003, 49 (04) :905-918
[45]   Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins [J].
Hoiczyk, E ;
Roggenkamp, A ;
Reichenbecher, M ;
Lupas, A ;
Heesemann, J .
EMBO JOURNAL, 2000, 19 (22) :5989-5999
[46]   Genetic analysis of functions involved in the late stages of biofilm development in Burkholderia cepacia H111 [J].
Huber, B ;
Riedel, K ;
Köthe, M ;
Givskov, M ;
Molin, S ;
Eberl, L .
MOLECULAR MICROBIOLOGY, 2002, 46 (02) :411-426
[47]   Distinct mechanisms of integrin binding by Yersinia pseudotuberculosis adhesins determine the phagocytic response of host macrophages [J].
Hudson, KJ ;
Bliska, JB ;
Bouton, AH .
CELLULAR MICROBIOLOGY, 2005, 7 (10) :1474-1489
[48]   Salmonella enterica serotype typhimurium fimbrial proteins serve as antigens during infection of mice [J].
Humphries, A ;
DeRidder, S ;
Bäumler, AJ .
INFECTION AND IMMUNITY, 2005, 73 (09) :5329-5338
[49]   Characterization of translocation pores inserted into plasma membranes by type III-secreted Esp proteins of enteropathogenic Escherichia coli [J].
Ide, T ;
Laarmann, S ;
Greune, L ;
Schillers, H ;
Oberleithner, H ;
Schmidt, MA .
CELLULAR MICROBIOLOGY, 2001, 3 (10) :669-679
[50]   MULTIPLE BETA-1-CHAIN INTEGRINS ARE RECEPTORS FOR INVASIN, A PROTEIN THAT PROMOTES BACTERIAL PENETRATION INTO MAMMALIAN-CELLS [J].
ISBERG, RR ;
LEONG, JM .
CELL, 1990, 60 (05) :861-871