The development of bactericidal yeast strains by expressing thePediococcus acidilactici pediocin gene (pedA) inSaccharomyces cerevisiae

Schoeman, Heidi; Vivier, Melané A.; Toit, Maret du; Dicks, Leon M. T.; Pretorius, Isak S.

doi:10.1002/(sici)1097-0061(19990615)15:8<647::aid-yea409>3.0.co;2-5

Cited by 100 publications

(48 citation statements)

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“…The development of bactericidal yeast strains by expressing class IIa bacteriocins such as pediocin PA-1/AcH (166) and plantaricin 423 has been successfully carried out with S. cerevisiae (181), which could provide a potential application for bacteriocin-producing yeast in beverage industries. On the other hand, the use of the methylotrophic yeast Pichia pastoris as a heterologous host for production of significant concentrations of class IIa bacteriocins has been assessed for enterocin P (74) and pediocin PA-1/AcH (13).…”

Section: Purification and Heterologous Production Of Class Iia Bactermentioning

confidence: 99%

The Continuing Story of Class IIa Bacteriocins

Drider

Fimland

Héchard

et al. 2006

Microbiol Mol Biol Rev

636

543

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SUMMARY Many bacteria produce antimicrobial peptides, which are also referred to as peptide bacteriocins. The class IIa bacteriocins, often designated pediocin-like bacteriocins, constitute the most dominant group of antimicrobial peptides produced by lactic acid bacteria. The bacteriocins that belong to this class are structurally related and kill target cells by membrane permeabilization. Despite their structural similarity, class IIa bacteriocins display different target cell specificities. In the search for new antibiotic substances, the class IIa bacteriocins have been identified as promising new candidates and have thus received much attention. They kill some pathogenic bacteria (e.g., Listeria) with high efficiency, and they constitute a good model system for structure-function analyses of antimicrobial peptides in general. This review focuses on class IIa bacteriocins, especially on their structure, function, mode of action, biosynthesis, bacteriocin immunity, and current food applications. The genetics and biosynthesis of class IIa bacteriocins are well understood. The bacteriocins are ribosomally synthesized with an N-terminal leader sequence, which is cleaved off upon secretion. After externalization, the class IIa bacteriocins attach to potential target cells and, through electrostatic and hydrophobic interactions, subsequently permeabilize the cell membrane of sensitive cells. Recent observations suggest that a chiral interaction and possibly the presence of a mannose permease protein on the target cell surface are required for a bacteria to be sensitive to class IIa bacteriocins. There is also substantial evidence that the C-terminal half penetrates into the target cell membrane, and it plays an important role in determining the target cell specificity of these bacteriocins. Immunity proteins protect the bacteriocin producer from the bacteriocin it secretes. The three-dimensional structures of two class IIa immunity proteins have been determined, and it has been shown that the C-terminal halves of these cytosolic four-helix bundle proteins specify which class IIa bacteriocin they protect against.

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Section: Purification and Heterologous Production Of Class Iia Bactermentioning

confidence: 99%

The Continuing Story of Class IIa Bacteriocins

Drider

Fimland

Héchard

et al. 2006

Microbiol Mol Biol Rev

636

543

View full text Add to dashboard Cite

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“…Because of this important feature, P. acidilactici has been studied for its pediocin production and its possible utilization in biopreservation processes (Schoeman et al, 1999 ;Stiles, 1996). In the last few years several studies have been carried out to investigate the mode of action of pediocin AcH\PA-1 and to obtain its expression in other species of LAB more suitable than P. acidilactici for the preparation of fermented dairy products (Chen et al, 1997 ;Chikindas et al, 1995 ;Fimland et al, 1996 ;Horn et al, 1998 ;Miller et al, 1998 ;Motlagh et al, 1992).…”

Section: Staphylococcus Aureus Clostridium Perfringens Andmentioning

confidence: 99%

Genomic subpopulations within the species Pediococcus acidilactici detected by multilocus typing analysis: relationships between pediocin AcH/PA-1 producing and non-producing strains The GenBank accession numbers for the sequences determined in this work are given in Table 4 T4 .

Mora¹,

Fortina²,

Parini³

et al. 2000

Microbiology

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A high degree of genetic polymorphism among P. acidilactici strains was highlighted by a multilocus typing approach analysing several housekeeping genes and by sampling the whole genome using random amplified polymorphic DNA (RAPD) fingerprint analysis performed by using a single primer pedA gene targeted in low-stringency amplification conditions. Restriction fragment length polymorphism of the rpoC, ldhD/L and mle genes, and a modified RAPD analysis, permitted the grouping of Pediococcus acidilactici strains in seven genotypes (I-VII). Genotypic results obtained by analysing housekeeping genes involved in the transcription/translation machinery and in primary metabolism were supported by phylogenetic analysis based on the partial 16S rDNA sequencing of a reference strain of each of the seven clusters obtained. Three of the seven genotypes detected showed relationships with pediocin AcH/PA-1 production and carbohydrate fermentation patterns : all pediocin-producing and sucrose-positive strains were grouped in genotype VII, melibiose-, sucrose-and raffinose-positive strains in genotype VI, and arabinose-positive strains in genotype V.

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“…However, because of the attachment of bacteriocin on yeast cells, the concentration of free pediocin in the yeast culture supernatant was undesirably low (Schoeman et al 1999). …”

Section: Exchanging Leader Peptidesmentioning

confidence: 99%