The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae.

doi:10.1006/jmbi.1998.2167

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Article

The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae.

Journal of molecular biology - 27 Nov 1998

Rossjohn J, Gilbert R J, Crane D, Morgan P J, Mitchell T J, Rowe A J, Andrew P W, Paton J C, Tweten R K, Parker M W

Abstract excerpt

Pneumolysin, a member of the thiol-activated cytolysin family of toxins, is a virulence factor from the Gram-positive bacterium Streptococcus pneumoniae. The toxin forms large oligomeric pores in cholesterol-containing membranes of eukaryotic cells. A plethora of biochemical and mutagenesis data have been published on pneumolysin, since its initial characterization in the 1930s. Here we present an homology model...

Topics

Amino Acid Sequence
Bacterial Proteins
Bacterial Toxins
Cholesterol
Circular Dichroism
Computer Simulation
Cytotoxins
Hemolysin Proteins
Liposomes
Models, Molecular
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Binding

Protein Structure, Secondary

Sequence Homology, Amino Acid

Spectrometry, Fluorescence

Static Electricity

Streptococcus pneumoniae

Source

Open in PubMed

Identifiers

PMID: 9813129
DOI: 10.1006/jmbi.1998.2167

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