| Autor: |
El-Gendy AO; Microbiology and Immunology Department, Faculty of Pharmacy, Beni-Suef University, Salah Salem Street, Beni Suef, 62511, Egypt. Ahmed.elgendy@pharm.bsu.edu.eg., Brede DA; Department of Chemistry, Biotechnology and Food Science, Laboratory of Microbial Gene Technology and Food Microbiology, Norwegian University of Life Sciences, Ås, Norway., Essam TM; Microbiology and Immunology Department and Biotechnology Centre, Faculty of Pharmacy, Cairo University, Cairo, Egypt., Amin MA; Microbiology and Immunology Department and Biotechnology Centre, Faculty of Pharmacy, Cairo University, Cairo, Egypt., Ahmed SH; Microbiology and Immunology Department, Faculty of Medicine, Assiut University, Asyût, Egypt., Holo H; Department of Chemistry, Biotechnology and Food Science, Laboratory of Microbial Gene Technology and Food Microbiology, Norwegian University of Life Sciences, Ås, Norway., Nes IF; Department of Chemistry, Biotechnology and Food Science, Laboratory of Microbial Gene Technology and Food Microbiology, Norwegian University of Life Sciences, Ås, Norway., Shamikh YI; Department of Microbiology and Immunology, Nahda University, Beni Suef, Egypt.; Department of Virology, Egypt Center for Research and Regenerative Medicine, Cairo, Egypt. |
| Abstrakt: |
Nosocomial infections caused by enterococci are an ongoing global threat. Thus, finding therapeutic agents for the treatment of such infections are crucial. Some Enterococcus faecalis strains are able to produce antimicrobial peptides called bacteriocins. We analyzed 65 E. faecalis isolates from 43 food samples and 22 clinical samples in Egypt for 17 common bacteriocin-encoding genes of Enterococcus spp. These genes were absent in 11 isolates that showed antimicrobial activity putatively due to bacteriocins (three from food, including isolate OS13, and eight from clinical isolates). The food-isolated E. faecalis OS13 produced bacteriocin-like inhibitory substances (BLIS) named enterocin OS13, which comprised two peptides (enterocin OS13α OS13β) that inhibited the growth of antibiotic-resistant nosocomial E. faecalis and E. faecium isolates. The molecular weights of enterocin OS13α and OS13β were determined as 8079 Da and 7859 Da, respectively, and both were heat-labile. Enterocin OS13α was sensitive to proteinase K, while enterocin OS13β was resistant. Characterization of E. faecalis OS13 isolate revealed that it belonged to sequence type 116. It was non-hemolytic, bile salt hydrolase-negative, gelatinase-positive, and sensitive to ampicillin, penicillin, vancomycin, erythromycin, kanamycin, and gentamicin. In conclusion, BLIS as enterocin OS13α and OS13β represent antimicrobial agents with activities against antibiotic-resistant enterococcal isolates. |
