This Article Full Text (PDF) Other Versions of this Article: JB.01092-06v1 189/2/627    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Jefferies, J. Articles by Mitchell, T. Search for Related Content PubMed PubMed Citation Articles by Jefferies, J. Articles by Mitchell, T.

 Previous Article  |  Next Article 

J. Bacteriol. doi:10.1128/JB.01092-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Identification of a secreted cholesterol dependent cytolysin (mitilysin) from Streptococcus mitis

Division of Infection and Immunity, Glasgow Biomedical Research Centre, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8TA, Scotland, United Kingdom; Infection Research Group, Level 9, Glasgow Dental Hospital, 378 Sauchiehall Street, Glasgow G2 3JZ, Scotland, United Kingdom

^* To whom correspondence should be addressed. Email: T.Mitchell{at}bio.gla.ac.uk.

	Abstract

We have detected a cholesterol-dependent cytolysin, (which we have named mitilysin) in a small number of S. mitis isolates. We have sequenced the mitilysin gene from 7 isolates of S. mitis. Comparisons with the pneumococcal pneumolysin gene genes show 15 amino acid substitutions. S. mitis appear to release mitilysin extracellularly. Certain alleles of mitilysin are not recognised by a monoclonal antibody raised to the related toxin pneumolysin. Based on ELISA and neutralisation assay results, one isolate of S. mitis may produce a further haemolytic toxin in addition to mitilysin. As genetic exchange is known to occur between S.mitis and S.pneumoniae, this may have implications for the development of vaccines or therapies for pneumococcal disease that are based on pneumolysin.