Literature DB >> 1930675

Pore-forming bacterial protein hemolysins (cytolysins).

V Braun1, T Focareta.   

Abstract

Protein toxins forming pores in biological membranes occur frequently in Gram-positive and Gram-negative bacteria. They kill either bacteria or eukaryotic cells (at most, a few seem to act on both groups of organisms). Most of the toxins affecting eukaryotes have clearly been shown to be related to the pathogenicity of the producing organisms. Toxin formation frequently involves a number of genes which encode the toxin polypeptide as well as proteins for toxin activation and secretion. Regulation of toxin production is usually coupled with that of the synthesis of a number of other virulence factors. Iron is the only known environmental factor that regulates transcription of a number of toxin genes by a Fur repressor-type mechanism, as has been originally described in Escherichia coli. Interestingly, the thiol-activated hemolysins (cytolysins) of Gram-positive bacteria contain a single cysteine which can be replaced by alanine without affecting the cytolytic activity. The Gram-negative hemolysins (cytolysins) are usually synthesized as precursor proteins, then covalently modified to yield an active hemolysin and secreted via specific export systems, which differ for various types of hemolysins.

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Year:  1991        PMID: 1930675     DOI: 10.3109/10408419109113511

Source DB:  PubMed          Journal:  Crit Rev Microbiol        ISSN: 1040-841X            Impact factor:   7.624


  36 in total

1.  Toxin production by Campylobacter spp.

Authors:  T M Wassenaar
Journal:  Clin Microbiol Rev       Date:  1997-07       Impact factor: 26.132

2.  Activation of Serratia marcescens hemolysin through a conformational change.

Authors:  Georg Walker; Ralf Hertle; Volkmar Braun
Journal:  Infect Immun       Date:  2004-01       Impact factor: 3.441

3.  In vitro activation of the Serratia marcescens hemolysin through modification and complementation.

Authors:  R Ondraczek; S Hobbie; V Braun
Journal:  J Bacteriol       Date:  1992-08       Impact factor: 3.490

4.  Molecular analysis of the tlyA gene in Campylobacter lari.

Authors:  Keiko Matsubara; Takuya Nakajima; John E Moore; Beverley C Millar; Tsugiya Murayama; Motoo Matsuda
Journal:  Folia Microbiol (Praha)       Date:  2015-04-24       Impact factor: 2.099

5.  Synthetic Studies of Glycosylphosphatidylinositol (GPI) Anchors and GPI-Anchored Peptides, Glycopeptides, and Proteins.

Authors:  Zhongwu Guo
Journal:  Curr Org Synth       Date:  2013-06-01       Impact factor: 1.975

6.  Intermedilysin, a novel cytotoxin specific for human cells secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess.

Authors:  H Nagamune; C Ohnishi; A Katsuura; K Fushitani; R A Whiley; A Tsuji; Y Matsuda
Journal:  Infect Immun       Date:  1996-08       Impact factor: 3.441

Review 7.  Pathogenesis of Proteus mirabilis Infection.

Authors:  Chelsie E Armbruster; Harry L T Mobley; Melanie M Pearson
Journal:  EcoSal Plus       Date:  2018-02

8.  A cytolysin encoded by Salmonella is required for survival within macrophages.

Authors:  S J Libby; W Goebel; A Ludwig; N Buchmeier; F Bowe; F C Fang; D G Guiney; J G Songer; F Heffron
Journal:  Proc Natl Acad Sci U S A       Date:  1994-01-18       Impact factor: 11.205

Review 9.  Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis.

Authors:  S M Jacobsen; D J Stickler; H L T Mobley; M E Shirtliff
Journal:  Clin Microbiol Rev       Date:  2008-01       Impact factor: 26.132

10.  Characterization of a pore-forming cytotoxin expressed by Salmonella enterica serovars typhi and paratyphi A.

Authors:  Jan Oscarsson; Marie Westermark; Sven Löfdahl; Björn Olsen; Helena Palmgren; Yoshimitsu Mizunoe; Sun Nyunt Wai; Bernt Eric Uhlin
Journal:  Infect Immun       Date:  2002-10       Impact factor: 3.441

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