Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway

被引:64
作者
Page, AL [1 ]
Sansonetti, P [1 ]
Parsot, C [1 ]
机构
[1] Inst Pasteur, INSERM, U389, Unite Pathogenie Microbienne Mol, F-75724 Paris 15, France
关键词
D O I
10.1046/j.1365-2958.2002.02835.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The type III secretion (TTS) pathway is used by numerous Gram-negative pathogens to inject virulence factors into eukaryotic cells. In addition to a functional TTS apparatus, secretion of effector proteins depends upon specific chaperones. Using a two-hybrid screen in yeast and a co-purification assay in Shigella flexneri, we demonstrated that Spa15, which is encoded by an operon for components of the TTS apparatus, is associated in the cytoplasm with three proteins that are secreted by the TTS pathway, IpaA, IpgB1 and OspC3. Spa15 was found to be necessary for stability of IpgB1 but not IpaA, and for secretion of IpaA molecules that were stored in the cytoplasm but not those that were synthesized while the secretion apparatus was active. The ability of Spa15 to associate with several non-homologous secreted proteins, the presence of Spa15 homologues in other TTS systems and the location of the corresponding genes within operons for components of the TTS apparatus suggest that Spa15 belongs to a new class of TTS chaperones.
引用
收藏
页码:1533 / 1542
页数:10
相关论文
共 51 条
[1]   Enteropathogenic Escherichia coli translocated intimin receptor, Tir, requires a specific chaperone for stable secretion [J].
Abe, A ;
de Grado, M ;
Pfuetzner, RA ;
Sánchez-SanMartín, C ;
DeVinney, R ;
Puente, JL ;
Strynadka, NCJ ;
Finlay, BB .
MOLECULAR MICROBIOLOGY, 1999, 33 (06) :1162-1175
[2]   ICSB - A SHIGELLA-FLEXNERI VIRULENCE GENE NECESSARY FOR THE LYSIS OF PROTRUSIONS DURING INTERCELLULAR SPREAD [J].
ALLAOUI, A ;
MOUNIER, J ;
PREVOST, MC ;
SANSONETTI, PJ ;
PARSOT, C .
MOLECULAR MICROBIOLOGY, 1992, 6 (12) :1605-1616
[3]   Secretion of Ipa proteins by Shigella flexneri: Inducer molecules and kinetics of activation [J].
Bahrani, FK ;
Sansonetti, PJ ;
Parsot, C .
INFECTION AND IMMUNITY, 1997, 65 (10) :4005-4010
[4]   CHARACTERIZATION OF B-CELL EPITOPES ON IPAB, AN INVASION-ASSOCIATED ANTIGEN OF SHIGELLA-FLEXNERI - IDENTIFICATION OF AN IMMUNODOMINANT DOMAIN RECOGNIZED DURING NATURAL INFECTION [J].
BARZU, S ;
NATO, F ;
ROUYRE, S ;
MAZIE, JC ;
SANSONETTI, P ;
PHALIPON, A .
INFECTION AND IMMUNITY, 1993, 61 (09) :3825-3831
[5]   The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes [J].
Blocker, A ;
Gounon, P ;
Larquet, E ;
Niebuhr, K ;
Cabiaux, V ;
Parsot, C ;
Sansonetti, P .
JOURNAL OF CELL BIOLOGY, 1999, 147 (03) :683-693
[6]   Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells:: Role of the SycE chaperone binding domain of YopE [J].
Boyd, AP ;
Lambermont, I ;
Cornelis, GR .
JOURNAL OF BACTERIOLOGY, 2000, 182 (17) :4811-4821
[7]   InvB is a type III secretion chaperone specific for SspA [J].
Bronstein, PA ;
Miao, EA ;
Miller, SI .
JOURNAL OF BACTERIOLOGY, 2000, 182 (23) :6638-6644
[8]   The virulence plasmid pWR100 and the repertoire of proteins secreted by the type III secretion apparatus of Shigella flexneri [J].
Buchrieser, C ;
Glaser, P ;
Rusniok, C ;
Nedjari, H ;
d'Hauteville, H ;
Kunst, F ;
Sansonetti, P ;
Parsot, C .
MOLECULAR MICROBIOLOGY, 2000, 38 (04) :760-771
[9]   LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism [J].
Cambronne, ED ;
Cheng, LW ;
Schneewind, O .
MOLECULAR MICROBIOLOGY, 2000, 37 (02) :263-273
[10]   THE ANTIFOLDING ACTIVITY OF SECB PROMOTES THE EXPORT OF THE ESCHERICHIA-COLI MALTOSE-BINDING PROTEIN [J].
COLLIER, DN ;
BANKAITIS, VA ;
WEISS, JB ;
BASSFORD, PJ .
CELL, 1988, 53 (02) :273-283