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Antifungal properties of durancins isolated from E nterococcus durans A 5‐11 and of its synthetic fragments
Author(s) -
Belguesmia Y.,
Choiset Y.,
Rabesona H.,
BaudyFloc'h M.,
Le Blay G.,
Haertlé T.,
Chobert J.M.
Publication year - 2013
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/lam.12037
Subject(s) - antifungal , enterococcus , microbiology and biotechnology , biology , bacteria , chemistry , antibiotics , genetics
The aim of this work was to study the antifungal properties of durancins isolated from E nterococcus durans A 5‐11 and of their chemically synthesized fragments. E nterococcus durans A 5‐11 is a lactic acid bacteria strain isolated from traditional M ongolian airag cheese. This strain inhibits the growth of several fungi including F usarium culmorum , P enicillium roqueforti and D ebaryomyces hansenii . It produces two bacteriocins: durancin A 5‐11a and durancin A 5‐11b, which have similar antimicrobial properties. The whole durancins A 5‐11a and A 5‐11b, as well as their N ‐ and C ‐terminal fragments were synthesized, and their antifungal properties were studied. C‐terminal fragments of both durancins showed stronger antifungal activities than other tested peptides. Treatment of D . hansenii LMSA 2.11.003 strain with 2 mmol l −1 of the synthetic peptides led to the loss of the membrane integrity and to several changes in the ultra‐structure of the yeast cells. Chemically synthesized durancins and their synthetic fragments showed different antimicrobial properties from each other. N‐terminal peptides show activities against both bacterial and fungal strains tested. C‐terminal peptides have specific activities against tested fungal strain and do not show antibacterial activity. However, the C ‐terminal fragment enhances the activity of the N ‐terminal fragment in the whole bacteriocins against bacteria. Significance and Impact of the Study Antifungal properties of durancins isolated from E nterococcus durans A 5‐11 and of their chemically synthesized fragments were determined. Treatment of D . hansenii LMSA 2.11.003 strain with 2 mmol l −1 of the synthetic peptides led to the loss of the membrane integrity and to several changes in the ultra‐structure of the yeast cells. This work contributes to improve understanding of molecular causes of antimicrobial activities of bacteriocins and their fragments. It may be proposed that the studied peptides affect all the yeast cellular and intramembranes including cytoplasmatic reticulum and nuclear and vacuolar membranes.