Enterocin F4-9, a Novel O-Linked Glycosylated Bacteriocin
Enterocin F4-9, a Novel O-Linked Glycosylated Bacteriocin
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DOI:
10.1128/aem.00940-15
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发表时间:
2015-07-01
影响因子:
4.4
通讯作者:
Sonomoto, Kenji
中科院分区:
文献类型:
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作者:
Maky, Mohamed Abdelfattah;Ishibashi, Naoki;Sonomoto, Kenji
Enterococcus faecalis F4-9 isolated from Egyptian salted-fermented fish produces a novel bacteriocin, termed enterocin F4-9. Enterocin F4-9 was purified from the culture supernatant by three steps, and its molecular mass was determined to be 5,516.6 Da by mass spectrometry. Amino acid and DNA sequencing showed that the propeptide consists of 67 amino acid residues, with a leader peptide containing a double glycine cleavage site to produce a 47-amino-acid mature peptide. Enterocin F4-9 is modified by two molecules of N-acetylglucosamine beta-O-linked to Ser37 and Thr46. The O-linked N-acetylglucosamine moieties are essential for the antimicrobial activity of enterocin F4-9. Further analysis of the enterocin F4-9 gene cluster identified enfC, which has high sequence similarity to a glycosyltransferase. The antimicrobial activity of enterocin F4-9 covered a limited range of bacteria, including, interestingly, a Gram-negative strain, Escherichia coli JM109. Enterocin F4-9 is sensitive to protease, active at a wide pH range, and moderately resistant to heat.