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Applied and Environmental Microbiology, May 2003, p. 2737-2747, Vol. 69, No. 5
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.5.2737-2747.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Purification and Characterization of Streptin, a Type A1 Lantibiotic Produced by Streptococcus pyogenes

Philip A. Wescombe and John R. Tagg*

Department of Microbiology, University of Otago, Dunedin, New Zealand

Received 30 September 2002/ Accepted 13 February 2003

Approximately 10% of Streptococcus pyogenes strains inhibit the growth of all nine indicators in a standardized streptococcal bacteriocin typing scheme. The present study has shown that this inhibitory profile, referred to as bacteriocin producer (P)-type 777 activity, is due to the type A1 lantibiotic streptin. Two major forms of streptin were purified to homogeneity from 95% acidified (pH 2) methanol extracts of S. pyogenes M25 cells by using a series of reversed-phase chromatographic separations. The fully processed form of streptin (streptin 1) is a 23-amino-acid peptide with a mass of 2,424 Da. The 2,821-Mr form of the peptide (streptin 2) has three additional amino acids (TPY) at the N terminus. Strain M25 extracts also contained small quantities of the streptin 1 and streptin 2 peptides in various stages of dehydration. Streptin 1 and streptin 2 were each capable of specifically inducing streptin production when added to strain M25 cultures. The streptin gene cluster resembled that of other type A1 lantibiotics but appeared to lack a streptin-specific proteinase gene. Although the streptin structural gene (srtA) was widespread within S. pyogenes, being detected in 40 of 58 strains, each representing a different M serotype, only 10 of these srtA-positive strains produced active streptin. The failure of some strains to express streptin was attributed to an ~4.5-kb deletion in their streptin loci, encompassing genes putatively encoding proteins involved in streptin processing (srtB and srtC) and transport (srtT). In other strains, srtA transcription appeared to be defective. No direct association could be detected between the production of streptin and the production of the lantibiotic-like hemolysin streptolysin S in strain M25.

* Corresponding author. Mailing address: Department of Microbiology, University of Otago, P.O. Box 56, Dunedin, New Zealand. Phone: 64-3-479-7714. Fax: 64-3-479-8540. E-mail: john.tagg{at}stonebow.otago.ac.nz.

Applied and Environmental Microbiology, May 2003, p. 2737-2747, Vol. 69, No. 5
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.5.2737-2747.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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