Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin

P J Morgan; G Harrison; P P Freestone; D Crane; A J Rowe; T J Mitchell; P W Andrew; R J Gilbert

doi:10.1016/s0014-5793(97)00838-7

Structural and functional characterisation of two proteolytic fragments of the bacterial protein toxin, pneumolysin

FEBS Lett. 1997 Aug 4;412(3):563-7. doi: 10.1016/s0014-5793(97)00838-7.

Authors

P J Morgan¹, G Harrison, P P Freestone, D Crane, A J Rowe, T J Mitchell, P W Andrew, R J Gilbert

Affiliation

¹ Department of Microbiology and Immunology, University of Leicester, UK.

PMID: 9276467
DOI: 10.1016/s0014-5793(97)00838-7

Abstract

Proteolytic cleavage of the bacterial protein toxin pneumolysin with protease K creates two fragments of 37 and 15 kDa. This paper describes the purification of these two fragments and their subsequent physical and biological characterisation. The larger fragment is directly involved in the cytolytic mechanism of this pore-forming protein, via membrane binding and self-association. The smaller fragment lacks ordered structure or discernible activity.

MeSH terms

Bacterial Proteins
Circular Dichroism
Endopeptidase K
Hemolysis
Hydrolysis
Liposomes / metabolism
Peptide Fragments / chemistry*
Peptide Fragments / isolation & purification
Peptide Fragments / physiology*
Protein Binding
Spectrometry, Fluorescence
Streptolysins / chemistry*
Streptolysins / isolation & purification
Streptolysins / physiology*
Structure-Activity Relationship

Substances

Bacterial Proteins
Liposomes
Peptide Fragments
Streptolysins
plY protein, Streptococcus pneumoniae
Endopeptidase K