Literature DB >> 9076742

SopA, the outer membrane protease responsible for polar localization of IcsA in Shigella flexneri.

C Egile1, H d'Hauteville, C Parsot, P J Sansonetti.   

Abstract

The spreading ability of Shigella flexneri, a facultative intracellular Gram-negative bacterium, within the host-cell cytoplasm is the result of directional assembly and accumulation of actin filaments at one pole of the bacterium. IcsA/VirG, the 120 kDa outer membrane protein that is required for intracellular motility, is located at the pole of the bacterium where actin polymerization occurs. Bacteria growing in laboratory media and within infected cells release a certain proportion of the surface-exposed IcsA after proteolytic cleavage. In this study, we report the characterization of the sopA gene which is located on the virulence plasmid and encodes the protein responsible for the cleavage of IcsA. The deduced amino acid sequence of SopA exhibits 60% identity with those of the OmpT and OmpP outer membrane proteases of Escherichia coli. The construction and phenotypic characterization of a sopA mutant demonstrated that SopA is required for exclusive polar localization of IcsA on the bacterial surface and proper expression of the motility phenotype in infected cells.

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Year:  1997        PMID: 9076742     DOI: 10.1046/j.1365-2958.1997.2871652.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  64 in total

1.  The C-terminal domain of the Bordetella pertussis autotransporter BrkA forms a pore in lipid bilayer membranes.

Authors:  J L Shannon; R C Fernandez
Journal:  J Bacteriol       Date:  1999-09       Impact factor: 3.490

2.  The sigA gene which is borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation.

Authors:  K Al-Hasani; I R Henderson; H Sakellaris; K Rajakumar; T Grant; J P Nataro; R Robins-Browne; B Adler
Journal:  Infect Immun       Date:  2000-05       Impact factor: 3.441

3.  Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA.

Authors:  L D Brandon; M B Goldberg
Journal:  J Bacteriol       Date:  2001-02       Impact factor: 3.490

Review 4.  Molecular basis of the intracellular spreading of Shigella.

Authors:  T Suzuki; C Sasakawa
Journal:  Infect Immun       Date:  2001-10       Impact factor: 3.441

5.  Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio.

Authors:  M Charles; M Pérez; J H Kobil; M B Goldberg
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-31       Impact factor: 11.205

6.  Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site.

Authors:  L Vandeputte-Rutten; R A Kramer; J Kroon; N Dekker; M R Egmond; P Gros
Journal:  EMBO J       Date:  2001-09-17       Impact factor: 11.598

Review 7.  Polarity in action: asymmetric protein localization in bacteria.

Authors:  S R Lybarger; J R Maddock
Journal:  J Bacteriol       Date:  2001-06       Impact factor: 3.490

8.  The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated.

Authors:  J W St Geme; D Cutter
Journal:  J Bacteriol       Date:  2000-11       Impact factor: 3.490

9.  Utilization of Escherichia coli outer-membrane endoprotease OmpT variants as processing enzymes for production of peptides from designer fusion proteins.

Authors:  Kazuaki Okuno; Masayuki Yabuta; Toshihiko Ooi; Shinichi Kinoshita
Journal:  Appl Environ Microbiol       Date:  2004-01       Impact factor: 4.792

Review 10.  Molecular and cellular mechanisms of invasion of the intestinal barrier by enteric pathogens. The paradigm of Shigella.

Authors:  P J Sansonetti
Journal:  Folia Microbiol (Praha)       Date:  1998       Impact factor: 2.099

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