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Appl. Environ. Microbiol., 11 1997, 4185-4190, Vol 63, No. 11
Copyright © 1997, American Society for Microbiology

Purification and characterization of staphylococcin BacR1, a broad- spectrum bacteriocin

SS Crupper, AJ Gies and JJ Iandolo
Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City 73190, USA.

The bacteriocin BacR1 was purified from culture supernatant of Staphylococcus aureus UT0007 by sequential ammonium sulfate precipitation, cation-exchange chromatography, and C4 reverse-phase chromatography steps. Mass spectrographic analysis indicated that the purified peptide has a molecular mass of 3,338 Da. It is resistant to environmental conditions, retaining full biological activity after exposure to pH extremes (pHs 3 to 11), heating at 95 degrees C for 15 min, and exposure to strong chaotropic agents. BacR1 was destroyed with a complete loss of biological activity after digestion with trypsin and proteinase K. Amino acid sequence analysis revealed a high concentration of Asx, Gly, and Pro residues and a high proportion of hydrophobic amino acids. The peptide is bactericidal and kills in a dose-dependent manner, but it does not lyse log-phase cells of Corynebacterium renale, the routine indicator organism for bacteriocin assay. A specific receptor for binding was detected on sensitive cells but not on insensitive cells. Competition assays showed that UV- inactivated cells could protect susceptible cells from antibacterial action. A partial inhibitory spectrum revealed that organisms from the following genera are susceptible: Staphylococcus, Streptococcus, Corynebacterium, Haemophilus, Bordetella, Moraxella, Pasteurella, Neisseria, and Bacillus.

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