Literature DB >> 8055936

Interaction of Serratia marcescens hemolysin (ShlA) with artificial and erythrocyte membranes. Demonstration of the formation of aqueous multistate channels.

R Schönherr1, M Hilger, S Broer, R Benz, V Braun.   

Abstract

Pore formation by hemolysin (ShlA) of Serratia marcescens was studied in erythrocytes and in artificial lipid bilayer membranes. The results with erythrocytes demonstrated that hemolysin pores varied in size. In erythrocyte membranes with reduced fluidity (0 degrees C), the toxin formed small pores with diameter 1-1.5 nm. In fluid membranes (above 20 degrees C), hemolysin pores with larger diameters (approximately 2.5-3.0 nm) were observed, which may be caused by association of ShlA monomers into oligomers. Comparison of the channels formed by Staphylococcus aureus alpha-toxin with channels formed by ShlA indicated a slightly smaller pore diameter of ShlA pores. Analysis of ShlA in artificial lipid bilayers showed the formation of pores with a broad distribution of single channel conductances, suggesting variable sizes of the ShlA pore. The lower limit for the pore diameter was approximately 1.0 nm. The ShlA pores did not exhibit pronounced ion selectivity nor voltage dependence, supporting the presence of a large water-filled pore.

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Year:  1994        PMID: 8055936     DOI: 10.1111/j.1432-1033.1994.tb19038.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  13 in total

1.  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

2.  Structural and functional studies of truncated hemolysin A from Proteus mirabilis.

Authors:  Todd M Weaver; Joshua A Smith; Jason M Hocking; Lucas J Bailey; Grayson T Wawrzyn; David R Howard; Laura A Sikkink; Marina Ramirez-Alvarado; James R Thompson
Journal:  J Biol Chem       Date:  2009-06-03       Impact factor: 5.157

Review 3.  Role of pore-forming toxins in bacterial infectious diseases.

Authors:  Ferdinand C O Los; Tara M Randis; Raffi V Aroian; Adam J Ratner
Journal:  Microbiol Mol Biol Rev       Date:  2013-06       Impact factor: 11.056

4.  Cytotoxic activities of Leptospira interrogans hemolysin SphH as a pore-forming protein on mammalian cells.

Authors:  Seoung Hoon Lee; Sangduk Kim; Seung Chul Park; Min Ja Kim
Journal:  Infect Immun       Date:  2002-01       Impact factor: 3.441

5.  Superlytic hemolysin mutants of Serratia marcescens.

Authors:  M Hilger; V Braun
Journal:  J Bacteriol       Date:  1995-12       Impact factor: 3.490

6.  Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1.

Authors:  H Ikigai; A Akatsuka; H Tsujiyama; T Nakae; T Shimamura
Journal:  Infect Immun       Date:  1996-08       Impact factor: 3.441

7.  Target cell range of Haemophilus ducreyi hemolysin and its involvement in invasion of human epithelial cells.

Authors:  G E Wood; S M Dutro; P A Totten
Journal:  Infect Immun       Date:  1999-08       Impact factor: 3.441

8.  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

9.  Serratia marcescens ShlA pore-forming toxin is responsible for early induction of autophagy in host cells and is transcriptionally regulated by RcsB.

Authors:  Gisela Di Venanzio; Tatiana M Stepanenko; Eleonora García Véscovi
Journal:  Infect Immun       Date:  2014-06-09       Impact factor: 3.441

10.  Cytotoxic action of Serratia marcescens hemolysin on human epithelial cells.

Authors:  R Hertle; M Hilger; S Weingardt-Kocher; I Walev
Journal:  Infect Immun       Date:  1999-02       Impact factor: 3.441

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