Outer membrane proteins of pathogenic spirochetes

被引:132
作者
Cullen, PA
Haake, DA
Adler, B [1 ]
机构
[1] Monash Univ, Dept Microbiol, Australian Bacterial Pathogenesis Program, Melbourne, Vic 3800, Australia
[2] Monash Univ, Victorian Bioinformat Consortium, Melbourne, Vic 3800, Australia
[3] Univ Calif Los Angeles, Sch Med, Los Angeles, CA 90095 USA
[4] Vet Affairs Greater Los Angeles Healthcare Syst, Div Infect Dis, Los Angeles, CA 90073 USA
关键词
pathogenic spirochetes; outer membrane proteins; lipoproteins; immunity; pathogenesis; surface exposure;
D O I
10.1016/j.femsre.2003.10.004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Pathogenic spirochetes are the causative agents of several important diseases including syphilis, Lyme disease, leptospirosis, swine dysentery, periodontal disease and some forms of relapsing fever. Spirochetal bacteria possess two membranes and the proteins present in the outer membrane are at the site of interaction with host tissue and the immune system. This review describes the current knowledge in the field of spirochetal outer membrane protein (OMP) biology. What is known concerning biogenesis and structure of OMPs, with particular regard to the atypical signal peptide cleavage sites observed amongst the spirochetes, is discussed. We examine the functions that have been determined for several spirochetal OMPs including those that have been demonstrated to function as adhesins, porins or to have roles in complement resistance. A detailed description of the role of spirochetal OMPs in immunity, including those that stimulate protective immunity or that are involved in antigenic variation, is given. A final section is included which covers experimental considerations in spirochetal outer membrane biology. This section covers contentious issues concerning cellular localization of putative OMPs, including determination of surface exposure. A more detailed knowledge of spirochetal OMP biology will hopefully lead to the design of new vaccines and a better understanding of spirochetal pathogenesis. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:291 / 318
页数:28
相关论文
共 315 条
[41]   THE VARIABLE ANTIGENS VMP7 AND VMP21 OF THE RELAPSING FEVER BACTERIUM BORRELIA-HERMSII ARE STRUCTURALLY ANALOGOUS TO THE VSG PROTEINS OF THE AFRICAN TRYPANOSOME [J].
BURMAN, N ;
BERGSTROM, S ;
RESTREPO, BI ;
BARBOUR, AG .
MOLECULAR MICROBIOLOGY, 1990, 4 (10) :1715-1726
[42]  
Busch RA, 1997, DEV BIOLOGICALS, V90, P245
[43]   VARIABILITY OF A BACTERIAL SURFACE PROTEIN AND DISEASE EXPRESSION IN A POSSIBLE MOUSE MODEL OF SYSTEMIC LYME BORRELIOSIS [J].
CADAVID, D ;
THOMAS, DD ;
CRAWLEY, R ;
BARBOUR, AG .
JOURNAL OF EXPERIMENTAL MEDICINE, 1994, 179 (02) :631-642
[44]   Immunologic and genetic analyses of VmpA of a neurotropic strain of Borrelia turicatae [J].
Cadavid, D ;
Pennington, PM ;
Kerentseva, TA ;
Bergstrom, S ;
Barbour, AG .
INFECTION AND IMMUNITY, 1997, 65 (08) :3352-3360
[45]   The Treponema denticola major sheath protein is predominantly periplasmic and has only limited surface exposure [J].
Caimano, MJ ;
Bourell, KW ;
Bannister, TD ;
Cox, DL ;
Radolf, JD .
INFECTION AND IMMUNITY, 1999, 67 (08) :4072-4083
[46]   Function and protective capacity of Treponema pallidum subsp. pallidum glycerophosphodiester phosphodiesterase [J].
Cameron, CE ;
Castro, C ;
Lukehart, SA ;
Van Voorhis, WC .
INFECTION AND IMMUNITY, 1998, 66 (12) :5763-5770
[47]   Identification of a Treponema pallidum laminin-binding protein [J].
Cameron, CE .
INFECTION AND IMMUNITY, 2003, 71 (05) :2525-2533
[48]   A FAMILY OF SURFACE-EXPOSED PROTEINS OF 20 KILODALTONS IN THE GENUS BORRELIA [J].
CARTER, CJ ;
BERGSTROM, S ;
NORRIS, SJ ;
BARBOUR, AG .
INFECTION AND IMMUNITY, 1994, 62 (07) :2792-2799
[49]   DbpA, but not OspA, is expressed by Borrelia burgdorferi during spirochetemia and is a target for protective antibodies [J].
Cassatt, DR ;
Patel, NK ;
Ulbrandt, ND ;
Hanson, MS .
INFECTION AND IMMUNITY, 1998, 66 (11) :5379-5387
[50]   Treponema pallidum major sheath protein homologue Tpr K is a target of opsonic antibody and the protective immune response [J].
Centurion-Lara, A ;
Castro, C ;
Barrett, L ;
Cameron, C ;
Mostowfi, M ;
Van Voorhis, WC ;
Lukehart, SA .
JOURNAL OF EXPERIMENTAL MEDICINE, 1999, 189 (04) :647-656