Abstract:
:In this work, we report the expression and secretion of the leaderless two-peptide (EntL50A and EntL50B) bacteriocin enterocin L50 from Enterococcus faecium L50 by the methylotrophic yeast Pichia pastoris X-33. The bacteriocin structural genes entL50A and entL50B were fused to the Saccharomyces cerevisiae gene region encoding the mating pheromone alpha-factor 1 secretion signal (MFalpha1(s)) and cloned, separately and together (entL50AB), into the P. pastoris expression and secretion vector pPICZalphaA, which contains the methanol-inducible alcohol oxidase promoter (P(AOX1)) to express the fusion genes. After transfer into the yeast, the recombinant plasmids were integrated into the genome, resulting in three bacteriocinogenic yeast strains able to produce and secrete the individual bacteriocin peptides EntL50A and EntL50B separately and together. The secretion was efficiently directed by MFalpha1(s) through the Sec system, and the precursor peptides were found to be correctly processed to form mature and active bacteriocin peptides. The present work describes for the first time the heterologous expression and secretion of a two-peptide non-pediocin-like bacteriocin by a yeast.
journal_name
Appl Environ Microbioljournal_title
Applied and environmental microbiologyauthors
Basanta A,Gómez-Sala B,Sánchez J,Diep DB,Herranz C,Hernández PE,Cintas LMdoi
10.1128/AEM.02206-09subject
Has Abstractpub_date
2010-05-01 00:00:00pages
3314-24issue
10eissn
0099-2240issn
1098-5336pii
AEM.02206-09journal_volume
76pub_type
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