Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 152 (2006), 1991-2001; DOI  10.1099/mic.0.28823-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Heng, N. C. K.
Right arrow Articles by Jack, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Heng, N. C. K.
Right arrow Articles by Jack, R. W.
Agricola
Right arrow Articles by Heng, N. C. K.
Right arrow Articles by Jack, R. W.
Microbiology 152 (2006), 1991-2001; DOI  10.1099/mic.0.28823-0
© 2006 Society for General Microbiology

Dysgalacticin: a novel, plasmid-encoded antimicrobial protein (bacteriocin) produced by Streptococcus dysgalactiae subsp. equisimilis

Nicholas C. K. Heng, Nancy L. Ragland, Pearl M. Swe, Hayley J. Baird, Megan A. Inglis, John R. Tagg and Ralph W. Jack

Department of Microbiology and Immunology, University of Otago, PO Box 56, Dunedin, New Zealand

Correspondence
Ralph W. Jack
ralph.jack{at}stonebow.otago.ac.nz

Dysgalacticin is a novel bacteriocin produced by Streptococcus dysgalactiae subsp. equisimilis strain W2580 that has a narrow spectrum of antimicrobial activity directed primarily against the principal human streptococcal pathogen Streptococcus pyogenes. Unlike many previously described bacteriocins of Gram-positive bacteria, dysgalacticin is a heat-labile 21.5 kDa anionic protein that kills its target without inducing lysis. The N-terminal amino acid sequence of dysgalacticin [Asn-Glu-Thr-Asn-Asn-Phe-Ala-Glu-Thr-Gln-Lys-Glu-Ile-Thr-Thr-Asn-(Asn)-Glu-Ala] has no known homologue in publicly available sequence databases. The dysgalacticin structural gene, dysA, is located on the indigenous plasmid pW2580 of strain W2580 and encodes a 220 aa preprotein which is probably exported via a Sec-dependent transport system. Natural dysA variants containing conservative amino acid substitutions were also detected by sequence analyses of dysA elements from S. dysgalactiae strains displaying W2580-like inhibitory profiles. Production of recombinant dysgalacticin by Escherichia coli confirmed that this protein is solely responsible for the inhibitory activity exhibited by strain W2580. A combination of in silico secondary structure prediction and reductive alkylation was employed to demonstrate that dysgalacticin has a novel structure containing a disulphide bond essential for its biological activity. Moreover, dysgalacticin displays similarity in predicted secondary structure (but not primary amino acid sequence or inhibitory spectrum) with another plasmid-encoded streptococcal bacteriocin, streptococcin A-M57 from S. pyogenes, indicating that dysgalacticin represents a prototype of a new class of antimicrobial proteins.


The GenBank/EMBL/DDBJ accession number for the pW2580 sequence determined in this paper is AY907345.




This article has been cited by other articles:


Home page
Antimicrob. Agents Chemother.Home page
E. Izquierdo, Y. Cai, E. Marchioni, and S. Ennahar
Genetic Identification of the Bacteriocins Produced by Enterococcus faecium IT62 and Evidence that Bacteriocin 32 Is Identical to Enterocin IT
Antimicrob. Agents Chemother., May 1, 2009; 53(5): 1907 - 1911.
[Abstract] [Full Text] [PDF]


Home page
J Antimicrob ChemotherHome page
P. M. Swe, G. M. Cook, J. R. Tagg, and R. W. Jack
Mode of action of dysgalacticin: a large heat-labile bacteriocin
J. Antimicrob. Chemother., April 1, 2009; 63(4): 679 - 686.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
E. Izquierdo, A. Bednarczyk, C. Schaeffer, Y. Cai, E. Marchioni, A. Van Dorsselaer, and S. Ennahar
Production of Enterocins L50A, L50B, and IT, a New Enterocin, by Enterococcus faecium IT62, a Strain Isolated from Italian Ryegrass in Japan
Antimicrob. Agents Chemother., June 1, 2008; 52(6): 1917 - 1923.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
P. M. Swe, N. C. K. Heng, Y.-T. Ting, H. J. Baird, A. Carne, A. Tauch, J. R. Tagg, and R. W. Jack
ef1097 and ypkK encode enterococcin V583 and corynicin JK, members of a new family of antimicrobial proteins (bacteriocins) with modular structure from Gram-positive bacteria
Microbiology, October 1, 2007; 153(10): 3218 - 3227.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2006 Society for General Microbiology.