Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18
<i>Pantoea 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...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2020-01-01
|
| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/25/3/485 |
| _version_ | 1819157438135271424 |
|---|---|
| author | Tieshan Teng Xianghui Li Lei Zhang Yanzhang Li |
| author_facet | Tieshan Teng Xianghui Li Lei Zhang Yanzhang Li |
| author_sort | Tieshan Teng |
| collection | DOAJ |
| description | <i>Pantoea 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 dispersa</i> W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from <i>Pantoea dispersa</i> 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 <i>Pantoea dispersa</i>. |
| first_indexed | 2024-12-22T16:08:46Z |
| format | Article |
| id | doaj.art-eb62895415b24bf284bb9b3125a47f08 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-22T16:08:46Z |
| publishDate | 2020-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-eb62895415b24bf284bb9b3125a47f082022-12-21T18:20:32ZengMDPI AGMolecules1420-30492020-01-0125348510.3390/molecules25030485molecules25030485Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18Tieshan Teng0Xianghui Li1Lei Zhang2Yanzhang Li3Joint National Laboratory for Antibody Drug Engineering, Institute of Biomedical Informatics, School of Basic Medical Sciences, Henan University, Kaifeng 475004, ChinaJoint National Laboratory for Antibody Drug Engineering, Institute of Biomedical Informatics, School of Basic Medical Sciences, Henan University, Kaifeng 475004, ChinaJoint National Laboratory for Antibody Drug Engineering, Institute of Biomedical Informatics, School of Basic Medical Sciences, Henan University, Kaifeng 475004, ChinaJoint National Laboratory for Antibody Drug Engineering, Institute of Biomedical Informatics, School of Basic Medical Sciences, Henan University, Kaifeng 475004, China<i>Pantoea 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 dispersa</i> W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from <i>Pantoea dispersa</i> 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 <i>Pantoea dispersa</i>.https://www.mdpi.com/1420-3049/25/3/485pantoea dispersapeptide natural productsmycobacterium tuberculosis |
| spellingShingle | Tieshan Teng Xianghui Li Lei Zhang Yanzhang Li Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18 Molecules pantoea dispersa peptide natural products mycobacterium tuberculosis |
| title | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18 |
| title_full | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18 |
| title_fullStr | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18 |
| title_full_unstemmed | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18 |
| title_short | Identification and Characterization of pantocin wh-1, a Novel Cyclic Polypeptide Produced by <i>Pantoea dispersa</i> W18 |
| title_sort | identification and characterization of pantocin wh 1 a novel cyclic polypeptide produced by i pantoea dispersa i w18 |
| topic | pantoea dispersa peptide natural products mycobacterium tuberculosis |
| url | https://www.mdpi.com/1420-3049/25/3/485 |
| work_keys_str_mv | AT tieshanteng identificationandcharacterizationofpantocinwh1anovelcyclicpolypeptideproducedbyipantoeadispersaiw18 AT xianghuili identificationandcharacterizationofpantocinwh1anovelcyclicpolypeptideproducedbyipantoeadispersaiw18 AT leizhang identificationandcharacterizationofpantocinwh1anovelcyclicpolypeptideproducedbyipantoeadispersaiw18 AT yanzhangli identificationandcharacterizationofpantocinwh1anovelcyclicpolypeptideproducedbyipantoeadispersaiw18 |