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Titolo:
Role of EscF, a putative needle complex protein, in the type III protein translocation system of enteropathogenic Escherichia coli
Autore:
Wilson, RK; Shaw, RK; Daniell, S; Knutton, S; Frankel, G;
Indirizzi:
Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, Ctr Mol Microbiol & Infect, London SW7 2AZ, England Univ London Imperial Coll Sci Technol& Med London England SW7 2AZ gland Univ Birmingham, Inst Child Hlth, Birmingham B4 6NH, W Midlands, England Univ Birmingham Birmingham W Midlands England B4 6NH W Midlands, England
Titolo Testata:
CELLULAR MICROBIOLOGY
fascicolo: 11, volume: 3, anno: 2001,
pagine: 753 - 762
SICI:
1462-5814(200111)3:11<753:ROEAPN>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPITHELIAL-CELLS; SECRETION SYSTEMS; SUPRAMOLECULAR STRUCTURE; ESPB PROTEIN; LOCUS; TIR; IDENTIFICATION; PATHOGENESIS; CHAPERONE; MEMBRANES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Frankel, G Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, CtrMol Microbiol & Infect, Flowers Bldg, London SW7 2AZ, England Univ London Imperial Coll Sci Technol & Med Flowers Bldg London England SW7 2AZ
Citazione:
R.K. Wilson et al., "Role of EscF, a putative needle complex protein, in the type III protein translocation system of enteropathogenic Escherichia coli", CELL MICROB, 3(11), 2001, pp. 753-762

Abstract

Type III secretion systems, designed to deliver effector proteins across the bacterial cell envelope and the plasma membrane of the target eukaryoticcell, are involved in subversion of eukaryotic cell functions in a varietyof human, animal and plant pathogens. In enteropathogenic Escherichia coli(EPEC), several protein substrates for the secretion apparatus were identified, including EspA, EspB and EspD. EspA is a structural protein and the major component of a large transiently expressed filamentous surface organelle that forms a direct link between the bacterium and the host cell, whereas EspD and EspB seem to form the mature translocation pore. Recent studies of the type III secretion systems of Shigella and Salmonella pathogenicity island (SPI)-1 revealed the existence of a macromolecular complex that spans both bacterial membranes and consists of a basal structure with two upperand two lower rings and a needle-like projection that extends outwards from the bacterial surface. MxiH (Shigella) and Prgl (Salmonella) are the maincomponents of the needle of the type III secretion complex. A needle-like complex has not yet been reported in EPEC. In this study, we investigated EscF, a protein sharing sequence similarity with MxiH and Prgl. We report that EscF is required for type III protein secretion and EspA filament assembly. Moreover, we show that EscF binds EspA, suggesting that EspA filaments are an extension of the type III secretion needle complexes in EPEC.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 03:33:17