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Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by Pantoea dispersa W18
Tieshan Teng1,2, Xianghui Li1, Lei Zhang1
1Joint National Laboratory for Antibody Drug Engineering, Institute of Biomedical Informatics, school of Basic Medical Sciences, Henan University, Kaifeng 475004, China.
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.
Insights
A soil bacterium, Pantoea dispersa W18, produces pantocin wh-1, a novel cyclic peptide with antimicrobial activity against Mycobacterium species, including tuberculosis. This discovery offers a potential new avenue for combating mycobacterial infections.
Area of Science:
- Microbiology
- Biochemistry
- Natural Product Chemistry
Background:
- * Pantoea dispersa W18, isolated from contaminated soil, exhibits antimicrobial properties.
- * Mycobacterium species, including Mycobacterium tuberculosis, are significant human pathogens.
Purpose of the Study:
- * To purify and identify the anti-mycobacterial compound produced by Pantoea dispersa W18.
- * To characterize the structure and properties of the identified compound.
Main Methods:
- * Purification using hydrophobic interaction chromatography, cation exchange chromatography, and reverse-phase HPLC.
- * Identification of the active compound through N-terminal amino acid sequencing.
- * Determination of molecular weight and structural features (cyclic peptide).
Main Results:
- * The anti-mycobacterial compound was identified as a cyclic peptide named pantocin wh-1 (1927 Da).
- * Pantocin wh-1 consists of 16 amino acid residues.
- * The peptide is heat-stable, unaffected by pH (2-12), inactivated by protease K, and partially by trypsin and pepsin.
Conclusions:
- * This study reports the first isolation and characterization of a cyclic polypeptide from Pantoea dispersa.
- * Pantocin wh-1 demonstrates significant antimicrobial activity against Mycobacterium species.
- * The unique properties of pantocin wh-1 suggest its potential as a novel therapeutic agent against tuberculosis.
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