Structure, function and regulation of Pseudomonas aeruginosa porins

被引:306
作者
Chevalier, Sylvie [1 ]
Bouffartigues, Emeline [1 ]
Bodilis, Josselin [1 ]
Maillot, Olivier [1 ]
Lesouhaitier, Olivier [1 ]
Feuilloley, Marc G. J. [1 ]
Orange, Nicole [1 ]
Dufour, Alain [2 ]
Cornelis, Pierre [1 ]
机构
[1] Normandy Univ, Univ Rouen, LMSM EA 4312, 55 Rue St Germain, F-27000 Evreux, France
[2] Univ Bretagne Sud UEB, IUEM, Lab Biotechnol & Chim Marines EA 3884, F-56321 Lorient, France
关键词
Pseudomonas aeruginosa; porins; OprF; regulation; virulence; outer membrane; OUTER-MEMBRANE-PROTEIN; GRAM-NEGATIVE BACTERIA; CYSTIC-FIBROSIS LUNG; VIRULENCE FACTOR PRODUCTION; GENOME-WIDE IDENTIFICATION; BASIC-AMINO-ACIDS; SIGMA-FACTOR SIGX; ESCHERICHIA-COLI; 2-COMPONENT SYSTEM; GENE-EXPRESSION;
D O I
10.1093/femsre/fux020
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Pseudomonas aeruginosa is a Gram-negative bacterium belonging to the gamma-proteobacteria. Like other members of the Pseudomonas genus, it is known for its metabolic versatility and its ability to colonize a wide range of ecological niches, such as rhizosphere, water environments and animal hosts, including humans where it can cause severe infections. Another particularity of P. aeruginosa is its high intrinsic resistance to antiseptics and antibiotics, which is partly due to its low outer membrane permeability. In contrast to Enterobacteria, pseudomonads do not possess general diffusion porins in their outer membrane, but rather express specific channel proteins for the uptake of different nutrients. The major outer membrane 'porin', OprF, has been extensively investigated, and displays structural, adhesion and signaling functions while its role in the diffusion of nutrients is still under discussion. Other porins include OprB and OprB2 for the diffusion of glucose, the two small outer membrane proteins OprG and OprH, and the two porins involved in phosphate/pyrophosphate uptake, OprP and OprO. The remaining nineteen porins belong to the so-called OprD (Occ) family, which is further split into two subfamilies termed OccD (8 members) and OccK (11 members). In the past years, a large amount of information concerning the structure, function and regulation of these porins has been published, justifying why an updated review is timely.
引用
收藏
页码:698 / 722
页数:25
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