Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from <i>Pollicipes pollicipes</i>
Crustins are a family of antimicrobial peptides (AMPs) that play a pivotal role in the innate immune system of crustaceans. The discovery of novel AMPs from natural sources is crucial for expanding our current database of these peptides. Here, we identified and characterized a novel member of the cr...
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MDPI AG
2024-11-01
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| author | Wei Zhang Liumi Wei Pengyu Chen Biao Ning Junjian Wang Peng He Chenjing Shang Dahui Yu |
| author_facet | Wei Zhang Liumi Wei Pengyu Chen Biao Ning Junjian Wang Peng He Chenjing Shang Dahui Yu |
| author_sort | Wei Zhang |
| collection | DOAJ |
| description | Crustins are a family of antimicrobial peptides (AMPs) that play a pivotal role in the innate immune system of crustaceans. The discovery of novel AMPs from natural sources is crucial for expanding our current database of these peptides. Here, we identified and characterized a novel member of the crustin family, named <i>Pp</i>Crus-SWD1, derived from <i>Pollicipes pollicipes</i>. <i>Pp</i>Crus-SWD1 consists of 138 amino acids and contains eight cysteine residues that form a conserved ‘four-disulfide core’ structure. Our recombinant <i>Pp</i>Crus-SWD1 (r<i>Pp</i>Crus-SWD1) exhibited potent inhibitory activity against three Gram-positive bacteria (<i>Staphylococcus aureus</i>, <i>Bacillus</i> sp. T2, and <i>Streptococcus agalactiae</i>) and six Gram-negative bacteria (<i>Aeromonas hydrophila</i>, <i>Escherichia coli</i>, <i>Vibrio anguillarum</i>, <i>Vibrio alginolyticus</i>, <i>Vibrio parahemolyticus</i>, and <i>Acinetobacter</i> sp. L3), with minimum inhibitory concentrations ranging from 16 to 64 μM. Furthermore, r<i>Pp</i>Crus-SWD1 demonstrated binding affinity towards both bacteria and pathogen-associated molecular patterns (PAMPs), and damaged bacterial barrier. Additionally, it effectively inhibited alkaline protease activity in <i>S. aureus</i> and <i>V. alginolyticus</i> strains. These findings highlight the potential utility of this newly discovered crustin as an effective alternative to antibiotics. |
| format | Article |
| id | doaj-art-5a29b4acf20a4e908ad80896db711292 |
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| issn | 1660-3397 |
| language | English |
| publishDate | 2024-11-01 |
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| series | Marine Drugs |
| spelling | doaj-art-5a29b4acf20a4e908ad80896db7112922025-08-20T02:00:47ZengMDPI AGMarine Drugs1660-33972024-11-01221252610.3390/md22120526Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from <i>Pollicipes pollicipes</i>Wei Zhang0Liumi Wei1Pengyu Chen2Biao Ning3Junjian Wang4Peng He5Chenjing Shang6Dahui Yu7Guangxi Key Laboratory of Marine Environmental Change and Disaster in Beibu Gulf, Beibu Gulf University, Qinzhou 535011, ChinaGuangxi Key Laboratory of Beibu Gulf Marine Biodiversity Conservation, Beibu Gulf University, Qinzhou 535011, ChinaEnvironmental Science, Shenzhen Engineering Laboratory for Marine Algal Biotechnology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, ChinaCollege of Marine Science BGU, Beibu Gulf University, Qinzhou 535011, ChinaGuangxi Key Laboratory of Marine Environmental Change and Disaster in Beibu Gulf, Beibu Gulf University, Qinzhou 535011, ChinaGuangxi Key Laboratory of Marine Environmental Change and Disaster in Beibu Gulf, Beibu Gulf University, Qinzhou 535011, ChinaEnvironmental Science, Shenzhen Engineering Laboratory for Marine Algal Biotechnology, Guangdong Provincial Key Laboratory for Plant Epigenetics, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen 518060, ChinaGuangxi Key Laboratory of Beibu Gulf Marine Biodiversity Conservation, Beibu Gulf University, Qinzhou 535011, ChinaCrustins are a family of antimicrobial peptides (AMPs) that play a pivotal role in the innate immune system of crustaceans. The discovery of novel AMPs from natural sources is crucial for expanding our current database of these peptides. Here, we identified and characterized a novel member of the crustin family, named <i>Pp</i>Crus-SWD1, derived from <i>Pollicipes pollicipes</i>. <i>Pp</i>Crus-SWD1 consists of 138 amino acids and contains eight cysteine residues that form a conserved ‘four-disulfide core’ structure. Our recombinant <i>Pp</i>Crus-SWD1 (r<i>Pp</i>Crus-SWD1) exhibited potent inhibitory activity against three Gram-positive bacteria (<i>Staphylococcus aureus</i>, <i>Bacillus</i> sp. T2, and <i>Streptococcus agalactiae</i>) and six Gram-negative bacteria (<i>Aeromonas hydrophila</i>, <i>Escherichia coli</i>, <i>Vibrio anguillarum</i>, <i>Vibrio alginolyticus</i>, <i>Vibrio parahemolyticus</i>, and <i>Acinetobacter</i> sp. L3), with minimum inhibitory concentrations ranging from 16 to 64 μM. Furthermore, r<i>Pp</i>Crus-SWD1 demonstrated binding affinity towards both bacteria and pathogen-associated molecular patterns (PAMPs), and damaged bacterial barrier. Additionally, it effectively inhibited alkaline protease activity in <i>S. aureus</i> and <i>V. alginolyticus</i> strains. These findings highlight the potential utility of this newly discovered crustin as an effective alternative to antibiotics.https://www.mdpi.com/1660-3397/22/12/526antimicrobial peptidescrustinantibacterial mechanism<i>Pollicipes pollicipes</i>antibiotic |
| spellingShingle | Wei Zhang Liumi Wei Pengyu Chen Biao Ning Junjian Wang Peng He Chenjing Shang Dahui Yu Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from <i>Pollicipes pollicipes</i> Marine Drugs antimicrobial peptides crustin antibacterial mechanism <i>Pollicipes pollicipes</i> antibiotic |
| title | Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from <i>Pollicipes pollicipes</i> |
| title_full | Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from <i>Pollicipes pollicipes</i> |
| title_fullStr | Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from <i>Pollicipes pollicipes</i> |
| title_full_unstemmed | Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from <i>Pollicipes pollicipes</i> |
| title_short | Discovery and Characterization of an Atypical Crustin Antimicrobial Peptide from <i>Pollicipes pollicipes</i> |
| title_sort | discovery and characterization of an atypical crustin antimicrobial peptide from i pollicipes pollicipes i |
| topic | antimicrobial peptides crustin antibacterial mechanism <i>Pollicipes pollicipes</i> antibiotic |
| url | https://www.mdpi.com/1660-3397/22/12/526 |
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