title: Aureocins 4185, bacteriocins produced by Staphylococcus aureus 4185: potential application in food preservation.
abstract: In the present study, the bacteriocins produced by Staphylococcus aureus 4185, a strain isolated from bovine mastitis, were purified and partially characterized. After purification by ammonium sulfate precipitation, cation-exchange chromatography, and five runs of high-performance liquid chromatography (HPLC), antimicrobial activity was recovered with 40% and 80% isopropanol, suggesting that more than one antimicrobial peptide, named aureocins 4185, is produced by S. aureus 4185. Mass spectrometry analyses revealed three peptides eluted with 40% isopropanol: peptide A (2,305.3 +/-1.5 Da), peptide B (2,327.3 +/-1.5 Da), and peptide C (3,005.5 +/-1.5 Da), and two peptides eluted with 80% isopropanol: peptide D (6,413.5 +/-1.5 Da) and peptide E (12,834.5 +/-1.5 Da). Although five peptides have been detected, only four small peptide sequences were obtained by matrix-assisted laser desorption/ionization time of flight (MALDI-TOF)/TOF mass spectrometry analyses: SLLEQFTGK (eluted with 40% isopropanol), ALLYDER, NNTSHNLPLGWFNVK, and NNLAQGTFNATK (eluted with 80% isopropanol). The sequences SLLEQFTGK and ALLYDER revealed identity with hypothetical peptides with unknown function. The sequences NNTSHNLPLGWFNVK and NNLAQGTFNATK showed similarity to a segment of a precursor of staphylococcal autolysins. The antimicrobial activity detected in the supernatant of strain 4185 proved to be resistant to heat treatment at 65°C; however, treatment at 80°C abolished completely its antimicrobial properties. The concentrated supernatant containing aureocins 4185 exhibited a strong bacteriolytic activity toward Micrococcus luteus ATCC 4698. Additionally, aureocins 4185 exhibited antagonistic activity against important foodborne pathogens, including Listeria monocytogenes, thus showing a potential application in food preservation.
authors.affiliation: Departamento de Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
authors.forename: Hilana
authors.initials: H
authors.lastname: Ceotto
authors.forename: Dag
authors.initials: D
authors.lastname: Brede
authors.forename: Zhian
authors.initials: Z
authors.lastname: Salehian
authors.forename: Janaína dos Santos
authors.initials: Jdos S
authors.lastname: Nascimento
authors.forename: Patricia Carlin
authors.initials: PC
authors.lastname: Fagundes
authors.forename: Ingolf F
authors.initials: IF
authors.lastname: Nes
authors.forename: Maria do Carmo de Freire
authors.initials: Mdo C
authors.lastname: Bastos
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000494:pharmacology*; D001409:Bacillus cereus / Q000187:drug effects; D001430:Bacteriocins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004355:Drug Stability; D005519:Food Preservation / Q000379:methods*; D006358:Hot Temperature; D007700:Kinetics; D008089:Listeria monocytogenes / Q000187:drug effects; D008414:Mastitis, Bovine / Q000382:microbiology; D016982:Micrococcus luteus / Q000187:drug effects; D008969:Molecular Sequence Data; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013211:Staphylococcus aureus / Q000378:metabolism*
chemical_list: D000890:Anti-Infective Agents; D001430:Bacteriocins