TY - JOUR
T1 - A novel bacteriocin-like substance (BLIS) from a pathogenic strain of Vibrio harveyi
AU - Prasad, Sathish
AU - Morris, Peter C.
AU - Hansen, Rasmus
AU - Meaden, Philip G.
AU - Austin, Brian
PY - 2005/9
Y1 - 2005/9
N2 - 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 pl of ~5.4 and a molecular mass of ~32 kDa. The N-terminal amino acid sequence of the protein comprised Asp-Glu-Tyr-lle-Ser-X-Asn-Lys-X-Ser-Ser-Ala-Asp-lle (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. © 2005 SGM.
AB - 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 pl of ~5.4 and a molecular mass of ~32 kDa. The N-terminal amino acid sequence of the protein comprised Asp-Glu-Tyr-lle-Ser-X-Asn-Lys-X-Ser-Ser-Ala-Asp-lle (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. © 2005 SGM.
UR - http://www.scopus.com/inward/record.url?scp=24944568592&partnerID=8YFLogxK
U2 - 10.1099/mic.0.28011-0
DO - 10.1099/mic.0.28011-0
M3 - Article
SN - 1350-0872
VL - 151
SP - 3051
EP - 3058
JO - Microbiology
JF - Microbiology
IS - 9
ER -