Streptolysin S-like virulence factors: the continuing sagA View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2011-08-08

AUTHORS

Evelyn M. Molloy, Paul D. Cotter, Colin Hill, Douglas A. Mitchell, R. Paul Ross

ABSTRACT

Key PointsThe operon that is responsible for the production, processing and export of streptolysin S (SLS), the post-translationally modified cytolytic toxin that causes the β-haemolytic phenotype of group A Streptococcus (GAS; also known as Streptococcus pyogenes), has been identified and characterized.Initial steps have been made towards the elucidation of the structure of SLS.SLS contributes to virulence through soft-tissue damage, its impact on host phagocytes and its role in the translocation of GAS across the epithelial barrier. It also functions as a signalling molecule, and there is speculation that it has a role in iron acquisition.It has become evident that SLS-like toxins are more widespread among streptococci than was previously appreciated; SLS-like toxins are produced by invasive human isolates of β-haemolytic group C and G streptococci, by the zoonotic fish pathogen Streptococcus iniae and by the horse pathogen Streptococcus equi.The SLS-like peptide family has been further extended to beyond the genus Streptococcus following the identification, initially using in silico approaches, of related gene clusters in a number of notorious Gram-positive pathogens, including Listeria monocytogenes, Clostridium botulinum and Staphylococcus aureus.SLS-like peptides belong to a recently defined large class of bioactive natural products known as thiazole/oxazole-modified microcins (TOMMs). TOMMs are characterized by a biosynthetic gene cluster that encodes a small precursor peptide and three adjacent synthetase proteins which serve to introduce thiazole, oxazole and methyloxazole heterocycles onto a ribosomally produced protoxin scaffold. More... »

PAGES

670-681

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nrmicro2624

DOI

http://dx.doi.org/10.1038/nrmicro2624

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019971854

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21822292


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