Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b
Fish are a potential source of diverse organic compounds with a broad spectrum of biological activities. Many fish-derived antimicrobial peptides and proteins are key components of the fish innate immune system. They are also potential candidates for development of new antimicrobial agents. CXCL20b...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-02-01
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| Series: | Antibiotics |
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| Online Access: | https://www.mdpi.com/2079-6382/9/2/78 |
| _version_ | 1818948170096312320 |
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| author | Xun Xiao Yanqi Zhang Zhiwei Liao Jianguo Su |
| author_facet | Xun Xiao Yanqi Zhang Zhiwei Liao Jianguo Su |
| author_sort | Xun Xiao |
| collection | DOAJ |
| description | Fish are a potential source of diverse organic compounds with a broad spectrum of biological activities. Many fish-derived antimicrobial peptides and proteins are key components of the fish innate immune system. They are also potential candidates for development of new antimicrobial agents. CXCL20b is a grass carp (<i>Ctenopharyngodon idella</i>) CXC chemokine strongly transcribed at the early stage of bacterial infections, for which the immune role had not been reported to date. In the present study, we found that CXCL20b is a cationic amphipathic protein that displays potent antimicrobial activity against both Gram-positive and Gram-negative bacteria. The results of DiOC<sub>2</sub>(3) and atomic force microscopy (AFM) assays indicated that CXCL20b could induce bacterial membrane depolarization and disruption in a short time. By performing further structure-activity studies, we found that the antimicrobial activity of CXCL20b was mainly relative to the N-terminal random coil region. The central part of this cytokine representing β-sheet region was insoluble in water and the C-terminal α-helical region did not show an antimicrobial effect. The results presented in this article support the poorly understood function of CXCL20b, which fulfills an important role in bony fish antimicrobial immunity. |
| first_indexed | 2024-12-20T08:42:32Z |
| format | Article |
| id | doaj.art-e2259ba9420842158461b765a017b001 |
| institution | Directory Open Access Journal |
| issn | 2079-6382 |
| language | English |
| last_indexed | 2024-12-20T08:42:32Z |
| publishDate | 2020-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj.art-e2259ba9420842158461b765a017b0012022-12-21T19:46:21ZengMDPI AGAntibiotics2079-63822020-02-01927810.3390/antibiotics9020078antibiotics9020078Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20bXun Xiao0Yanqi Zhang1Zhiwei Liao2Jianguo Su3Department of Aquatic Animal Medicine, College of Fisheries, Huazhong Agricultural University, No. 1 Shizishan St., Wuhan 430070, ChinaDepartment of Aquatic Animal Medicine, College of Fisheries, Huazhong Agricultural University, No. 1 Shizishan St., Wuhan 430070, ChinaDepartment of Aquatic Animal Medicine, College of Fisheries, Huazhong Agricultural University, No. 1 Shizishan St., Wuhan 430070, ChinaDepartment of Aquatic Animal Medicine, College of Fisheries, Huazhong Agricultural University, No. 1 Shizishan St., Wuhan 430070, ChinaFish are a potential source of diverse organic compounds with a broad spectrum of biological activities. Many fish-derived antimicrobial peptides and proteins are key components of the fish innate immune system. They are also potential candidates for development of new antimicrobial agents. CXCL20b is a grass carp (<i>Ctenopharyngodon idella</i>) CXC chemokine strongly transcribed at the early stage of bacterial infections, for which the immune role had not been reported to date. In the present study, we found that CXCL20b is a cationic amphipathic protein that displays potent antimicrobial activity against both Gram-positive and Gram-negative bacteria. The results of DiOC<sub>2</sub>(3) and atomic force microscopy (AFM) assays indicated that CXCL20b could induce bacterial membrane depolarization and disruption in a short time. By performing further structure-activity studies, we found that the antimicrobial activity of CXCL20b was mainly relative to the N-terminal random coil region. The central part of this cytokine representing β-sheet region was insoluble in water and the C-terminal α-helical region did not show an antimicrobial effect. The results presented in this article support the poorly understood function of CXCL20b, which fulfills an important role in bony fish antimicrobial immunity.https://www.mdpi.com/2079-6382/9/2/78chemokine<i>ctenopharyngodon idella</i>antimicrobial peptidemembrane permeabilization |
| spellingShingle | Xun Xiao Yanqi Zhang Zhiwei Liao Jianguo Su Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b Antibiotics chemokine <i>ctenopharyngodon idella</i> antimicrobial peptide membrane permeabilization |
| title | Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b |
| title_full | Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b |
| title_fullStr | Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b |
| title_full_unstemmed | Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b |
| title_short | Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b |
| title_sort | characterization and antimicrobial activity of the teleost chemokine cxcl20b |
| topic | chemokine <i>ctenopharyngodon idella</i> antimicrobial peptide membrane permeabilization |
| url | https://www.mdpi.com/2079-6382/9/2/78 |
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