Wide-inhibitory spectra bacteriocins produced by Lactobacillus gasseri K7

Zorič Peternel, Metoda (author), Čanžek Majhenič, Andreja (author), Holo, Helge (author), Nes, Ingolf (author), Salehian, Zhian (author), Berlec, Aleš (author), Rogelj, Irena (author)

The aim of study was to determine the genetic characterization and classification of Lb. gasseri K7 bacteriocins, comparison with bacteriocins of the Lb. gasseri LF221 strain and other related strains. Bacteriocin-encoding genes were amplified by PCR, subjected to DNA sequencing, and BLAST sequence analysis was performed to search the database for homologous peptides. Lb. gasseri K7 produces two-peptide bacteriocins, named gassericin K7 A and gasserin K7 B. Their nucleotide sequences were deposited at GenBank, under accession numbers EF392861 for the gassericin K7 A and AY307382 for the gassericin K7 B. Analysis of geneclausters of bacteriocins in Lb. gasseri K7 strain revealed a 100 percent sequence identity with bacteriocins in LF221 strain. An active peptide of gassericin K7 B is homologous to the complementary peptide of gassericin T, and a complementary peptide of gassericin K7 B is homologous to the active peptide of gassercin T. Another surprising finding was that the sakacin T0beta peptide is partly homologous to the active peptide of gassercin K7 A, while the other sakacin T peptide (alfa) is partly homologous to the complementary peptide of gassericin K7 B. Gassericins of Lb. gasseri K7 strain were both classified as two-peptide bacteriocins. Human probiotic strains Lb. gasseri K7 and LF221 aredifferent isolates but with identical bacteriocin genes. They produce wide-inhibitory spectra bacteriocins that are new members of two-peptide bacteriocins with some homologies to other bacteriocins in this group. Described bacteriocins offer a great potential in applications in food industry, pharmacy and biomedicine.

• Language: English
• Keywords: mikrobiologija, molekularna genetika, bakteriocini, Lactobacillus gasseri K7
• Work type: Not categorized
• Typology: 1.01 - Original Scientific Article
• Organization: BF - Biotechnical Faculty
• Year: 2010
• Number of pages: Str. 233-240
• Numbering: Vol. 2, no. 4
• PID: 20.500.12556/RUL-36520
• UDC: 579
• ISSN on article: 1867-1306
• DOI: 10.1007/s12602-010-9044-5
• COBISS.SI-ID: 2646920
• Publication date in RUL: 10.07.2015

Record is a part of a journal

• Title: Probiotics and antimicrobial proteins
• Shortened title: Probiot. antimicrob. proteins
• Publisher: Springer
• ISSN: 1867-1306
• COBISS.SI-ID: 2645640