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Bovicin HC5, a bacteriocin from Streptococcus bovis HC5
Hilário C Mantovani1, Haijing Hu1, Randy W Worobo1
1Section of Microbiology1 and Department of Food Science and Technology (NYSAES)2, Cornell University, Ithaca, NY 14853, USA.
Microbiology (Reading, England)
|November 13, 2002
Summary
Streptococcus bovis HC5 produces a novel pore-forming peptide bacteriocin, bovicin HC5, with broad Gram-positive antibacterial activity. This compound shows potential as a feed additive, inhibiting even nisin-resistant bacteria.
Area of Science:
- Microbiology
- Bacteriology
- Biochemistry
Background:
- * Streptococcus bovis HC5 exhibits potent antibacterial activity against Gram-positive bacteria.
- * The activity spectrum resembles that of monensin, a common feed additive.
- * Previous studies suggested inhibition of nisin-resistant strains.
Purpose of the Study:
- * To characterize the antibacterial agent produced by Streptococcus bovis HC5.
- * To determine the nature and mechanism of action of the active compound.
- * To elucidate the molecular properties and sequence of the bacteriocin.
Main Methods:
- * Crude extract preparation via ammonium sulfate precipitation.
- * Antibacterial activity assays and characterization of enzyme resistance (Pronase E, trypsin, proteinase K, alpha-chymotrypsin).
- * Extraction using acidic NaCl, potassium efflux assays, High-Performance Liquid Chromatography (HPLC) purification, and Matrix-Assisted Laser Desorption Ionization Time-of-Flight (MALDI-TOF) mass spectrometry.
- * Edman degradation for N-terminal sequencing.
Main Results:
- * The antibacterial activity was attributed to a cell-associated, pore-forming peptide.
- * The peptide was purified and found to have a molecular mass of approximately 2440 Da.
- * Partial N-terminal sequencing revealed a novel sequence (VGXRYASXPGXSWKYVXF) with similarities to lantibiotics, but distinct characteristics.
Conclusions:
- * Streptococcus bovis HC5 produces a novel bacteriocin, designated bovicin HC5.
- * Bovicin HC5 acts via pore formation, leading to potassium efflux.
- * The unique structure suggests a novel class of bacteriocins with potential applications.