Literature DB >> 9382829

Toxin structure: part of a hole?

H Bayley1.   

Abstract

The structure of the monomeric form of perfringolysin O solved by X-ray crystallography has been used to model the very large transmembrane pore formed when this bacterial protein toxin assembles in cholesterol-containing membranes. The structure is a notable advance, but it may not provide the whole story.

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Year:  1997        PMID： 9382829     DOI： 10.1016/s0960-9822(06)00399-x

Source DB:  PubMed          Journal:  Curr Biol        ISSN： 0960-9822            Impact factor:   10.834


  11 in total

1.  Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.

Authors:  George Miles; Liviu Movileanu; Hagan Bayley
Journal:  Protein Sci       Date:  2002-04       Impact factor: 6.725

2.  Role of listeriolysin O in cell-to-cell spread of Listeria monocytogenes.

Authors:  M M Gedde; D E Higgins; L G Tilney; D A Portnoy
Journal:  Infect Immun       Date:  2000-02       Impact factor: 3.441

3.  Protein arcs may form stable pores in lipid membranes.

Authors:  Lidia Prieto; Yi He; Themis Lazaridis
Journal:  Biophys J       Date:  2014-01-07       Impact factor: 4.033

4.  Inducible control of virulence gene expression in Listeria monocytogenes: temporal requirement of listeriolysin O during intracellular infection.

Authors:  Christina E Dancz; Andrea Haraga; Daniel A Portnoy; Darren E Higgins
Journal:  J Bacteriol       Date:  2002-11       Impact factor: 3.490

5.  A combined use of autolysin p60 and listeriolysin O antigens induces high protective immune responses against Listeria monocytogenes infection.

Authors:  Xuenong Luo; Xuepeng Cai
Journal:  Curr Microbiol       Date:  2012-09-23       Impact factor: 2.188

6.  Listeriolysin O as cytotoxic component of an immunotoxin.

Authors:  Sabine Bergelt; Stefan Frost; Hauke Lilie
Journal:  Protein Sci       Date:  2009-06       Impact factor: 6.725

Review 7.  Molecular features of the cytolytic pore-forming bacterial protein toxins.

Authors:  J E Alouf
Journal:  Folia Microbiol (Praha)       Date:  2003       Impact factor: 2.629

8.  Human perforin employs different avenues to damage membranes.

Authors:  Tilen Praper; Andreas Sonnen; Gabriella Viero; Ales Kladnik; Christopher J Froelich; Gregor Anderluh; Mauro Dalla Serra; Robert J C Gilbert
Journal:  J Biol Chem       Date:  2010-10-02       Impact factor: 5.157

9.  The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells.

Authors:  Ian J Glomski; Margaret M Gedde; Albert W Tsang; Joel A Swanson; Daniel A Portnoy
Journal:  J Cell Biol       Date:  2002-03-18       Impact factor: 10.539

10.  Carboxyl-Terminal Residues N478 and V479 Required for the Cytolytic Activity of Listeriolysin O Play a Critical Role in Listeria monocytogenes Pathogenicity.

Authors:  Changyong Cheng; Li Jiang; Tiantian Ma; Hang Wang; Xiao Han; Jing Sun; Yongchun Yang; Zhongwei Chen; Huifei Yu; Yi Hang; Fengdan Liu; Bosen Wang; Weihuan Fang; Huarong Huang; Chun Fang; Chang Cai; Nancy Freitag; Houhui Song
Journal:  Front Immunol       Date:  2017-11-01       Impact factor: 7.561
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