Bacteriocins of Lactobacillus gasseri K7 – Monitoring of gassericin K7 A and B genes’ expression and isolation of an active component

• Published in: Process biochemistry (1991) Vol. 49; no. 8; pp. 1251 - 1259
• Main Authors: Mavrič, Anja, Tompa, Gorazd, Trmčić, Aljoša, Rogelj, Irena, Bogovič Matijašić, Bojana
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01-08-2014
• Subjects: Bacteriocin expression; Gassericins K7; Lactobacillus gasseri; LC–MS/MS; MALDI-TOF; RT-qPCR; MALDI-TOF; RT-qPCR; LC–MS/MS; Gassericins K7; Bacteriocin expression; Lactobacillus gasseri
• ISSN: 1359-5113; 1873-3298
• DOI: 10.1016/j.procbio.2014.04.022

•Eight genes of L. gasseri K7 A and B bacteriocins were expressed during growth.•Developed isolation protocol enabled efficient recovery of gassericin K7 B.•The active component of gassericin K7 B was verified at the proteomic level.•The isolated peptide showed a broad spectrum of antimicrobial activity.
The genome of Lactobacillus gasseri K7, isolated from baby's faeces, contains gene regions encoding two-component bacteriocins named gassericin K7 A (GenBank EF392861) and gassericin K7 B (GenBank AY307382). The strain has been known to exhibit bacteriocin activity in vitro, however, no data exist on the expression of particular genes of bacteriocins’ operons or on the activity of individual components of this bacteriocin complex, which has not been isolated so far. The objectives of this study were to examine bacteriocin genes’ expression during the growth of L. gasseri K7 and to isolate individual components in order to reveal the contribution of individual peptides to the overall bacteriocin activity. All eight target genes were expressed during exponential phase of growth in MRS broth. Mass spectrometry analysis revealed that the amino acid sequence of isolated peptide matched the deduced amino acid sequence of putative active peptide of gassericin K7 B (Gas K7 B_AcP) and GatX, a complementary peptide of gassericin T, previously supposed to have no antimicrobial activity. The isolated peptide showed a broad spectrum of antimicrobial activity. Furthermore, the isolation protocol developed in this study will enable to obtain a considerable amount of purified bacteriocins needed for further investigation of their functionality.