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


     

Microbiology 151 (2005), 3051-3058; DOI  10.1099/mic.0.28011-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Table
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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Prasad, S.
Right arrow Articles by Austin, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Prasad, S.
Right arrow Articles by Austin, B.
Agricola
Right arrow Articles by Prasad, S.
Right arrow Articles by Austin, B.
Microbiology 151 (2005), 3051-3058; DOI  10.1099/mic.0.28011-0
© 2005 Society for General Microbiology

A novel bacteriocin-like substance (BLIS) from a pathogenic strain of Vibrio harveyi

Sathish Prasad, Peter C. Morris, Rasmus Hansen, Philip G. Meaden and Brian Austin

School of Life Sciences, John Muir Building, Heriot-Watt University, Riccarton, Edinburgh EH14 4AS, UK

Correspondence
Brian Austin
b.austin{at}hw.ac.uk

Inter-strain and inter-species inhibition mediated by a bacteriocin-like inhibitory substance (BLIS) from a pathogenic Vibrio harveyi strain VIB 571 was demonstrated against four isolates of the same species, and one culture each of a Vibrio sp., Vibrio fischeri, Vibrio gazogenes and Vibrio parahaemolyticus. The crude BLIS, which was obtained by ammonium-sulphate precipitation of the cell-free supernatant of a 72 h broth culture of strain VIB 571, was inactivated by lipase, proteinase K, pepsin, trypsin, pronase E, SDS and incubation at >=60 °C for 10 min. The activity was stable between pH 2–11 for at least 5 h. Anion-exchange chromatography, gel filtration, SDS-PAGE and two-dimensional gel electrophoresis revealed the presence of a single major peak, comprising a protein with a pI of ~5·4 and a molecular mass of ~32 kDa. The N-terminal amino acid sequence of the protein comprised Asp-Glu-Tyr-Ile-Ser-X-Asn-Lys-X-Ser-Ser-Ala-Asp-Ile (with X representing cysteine or modified amino acid residues). A similarity search based on the matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) generated peptide masses and the N-terminal sequence did not yield any significant matches.

Abbreviations: BLIS, bacteriocin-like inhibitory substance; CFS, cell-free supernatant; 2-DE, two-dimensional gel electrophoresis; DLPA, double-layer plate assay; MALDI-TOF-MS, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

A table of the bacterial isolates used in this study is available as suplementary data with the online version of the journal.






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 © 2005 Society for General Microbiology.