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Purification and structure of mutacin B‐Ny266: a new lantibiotic produced by Streptococcus mutans
Author(s) -
Mota-Meira Marilaine,
Lacroix Christophe,
LaPointe Gisèle,
Lavoie Marc C.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00425-0
Subject(s) - lantibiotics , edman degradation , streptococcus mutans , chemistry , chromatography , amino acid , biochemistry , molecular mass , peptide sequence , bacteriocin , bacteria , biology , organic chemistry , gene , enzyme , genetics , antimicrobial
Mutacins are bactericidal substances of proteinaceous nature produced by Streptococcus mutans . Lantibiotics are antibacterial substances containing post‐translationally modified amino acids such as lanthionine. Mutacin B‐Ny266 was purified from the cell pellet of S. mutans strain Ny266 by ethanol extraction at pH 2.0 followed by reversed‐phase chromatography (Sep‐Pak® cartridge) and by HPLC on a C 18 column. The mean purification factor was 3240±81 and the mean yield was 1.0±0.1%. Molecular mass of mutacin B‐Ny266 as determined by mass spectroscopy is 2270.29±0.21 Da. The amino acid sequence of the purified active fraction was obtained by Edman degradation after treatment with alkaline ethanethiol. Twenty‐one amino acids were detected in this analysis. Mutacin B‐Ny266 belongs to the type A lantibiotics. The proposed sequence is: F–K– –W–U–F– – –P–G– –A–K–O–G– –F–N– –Y– . The molecule differs from that of epidermin/staphylococcin 1580 and gallidermin at positions 1, 2, 4, 5 and 6.