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Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18.


ABSTRACT: Pantoea dispersa W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including Mycobacterium tuberculosis, an important human pathogen. Here, the anti-mycobacterial compound produced by Pantoea dispersa W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from Pantoea dispersa W18 were identified as a natural peptide named pantocin wh-1 with a 1927 Da molecular weight. The primary structure of this compound was detected by N-terminal amino acid sequencing. The amino acid sequence of pantocin wh-1 consisted of 16 amino acid residues with a cyclic structure. The pantocin wh-1 could be inactivated by protease K, but was heat stable and unaffected by pH (2-12). However, the activity was not completely inactivated by trypsin and pepsin. This is the first report of a cyclic polypeptide purified from a strain of Pantoea dispersa.

SUBMITTER: Teng T 

PROVIDER: S-EPMC7036871 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

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Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18.

Teng Tieshan T   Li Xianghui X   Zhang Lei L   Li Yanzhang Y  

Molecules (Basel, Switzerland) 20200123 3


<i>Pantoea</i> <i>dispersa</i> W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including <i>Mycobacterium tuberculosis</i>, an important human pathogen. Here, the anti-mycobacterial compound produced by <i>Pantoea</i> <i>dispersa</i> W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from <i>Pantoea</i> <i>dispersa</i> W18 were identifi  ...[more]

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