A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis
Antimicrobial peptides (AMPs) are crucial immune effectors in the defense against pathogens. Crustins, small molecule antimicrobial peptides found in crustaceans, exhibit antimicrobial and antiviral properties, microbial binding ability, biofilm growth inhibition, and protease inhibition. In this st...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-06-01
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| Series: | Comparative Immunology Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2950311625000321 |
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| author | Dandan Feng Zhu Zhu Shangpeng Wang Yangcan Gao Yingwen Li Yuying Sun Jiquan Zhang |
| author_facet | Dandan Feng Zhu Zhu Shangpeng Wang Yangcan Gao Yingwen Li Yuying Sun Jiquan Zhang |
| author_sort | Dandan Feng |
| collection | DOAJ |
| description | Antimicrobial peptides (AMPs) are crucial immune effectors in the defense against pathogens. Crustins, small molecule antimicrobial peptides found in crustaceans, exhibit antimicrobial and antiviral properties, microbial binding ability, biofilm growth inhibition, and protease inhibition. In this study, we identify and characterize a crustin (named NdCrus1) from Neocaridina denticulata sinensis. The NdCrus1 was expressed in all tested tissues, with the highest expression in the stomach. NdCrus1 shares a high identity with type I crustins and contains a whey acidic protein (WAP) domain, featuring eight cysteine residues that form the conserved ‘‘four-disulfide core’’ structure. Recombinant NdCrus1 (rNdCrus1) did not significantly inhibit Bacillus subtilis and Vibrio parahaemolyticus but possessed an inhibitory effect on proteases under a wide range of temperature conditions. In addition, in vitro binding assays and molecular docking results indicated that NdCrus1 had a strong binding capacity with chitin. These results provide new insights into crustins in the life activities of N. denticulata sinensis and provide references for studying antibacterial activity characteristics and mechanisms in other crustaceans. |
| format | Article |
| id | doaj-art-41c2b4e2c2064365a281eac22106b10c |
| institution | OA Journals |
| issn | 2950-3116 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Comparative Immunology Reports |
| spelling | doaj-art-41c2b4e2c2064365a281eac22106b10c2025-08-20T02:31:12ZengElsevierComparative Immunology Reports2950-31162025-06-01820022610.1016/j.cirep.2025.200226A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensisDandan Feng0Zhu Zhu1Shangpeng Wang2Yangcan Gao3Yingwen Li4Yuying Sun5Jiquan Zhang6School of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding 071002, ChinaSchool of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding 071002, ChinaSchool of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding 071002, ChinaSchool of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding 071002, ChinaSchool of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding 071002, ChinaSchool of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding 071002, China; Key Laboratory of Microbial Diversity Research and Application of Hebei Province, Baoding 071002, China; Engineering Research Center of Microbial Breeding and Conservation, Baoding 071002, China; Corresponding author at: School of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding 071002, China.School of Life Sciences/Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding 071002, China; Corresponding author.Antimicrobial peptides (AMPs) are crucial immune effectors in the defense against pathogens. Crustins, small molecule antimicrobial peptides found in crustaceans, exhibit antimicrobial and antiviral properties, microbial binding ability, biofilm growth inhibition, and protease inhibition. In this study, we identify and characterize a crustin (named NdCrus1) from Neocaridina denticulata sinensis. The NdCrus1 was expressed in all tested tissues, with the highest expression in the stomach. NdCrus1 shares a high identity with type I crustins and contains a whey acidic protein (WAP) domain, featuring eight cysteine residues that form the conserved ‘‘four-disulfide core’’ structure. Recombinant NdCrus1 (rNdCrus1) did not significantly inhibit Bacillus subtilis and Vibrio parahaemolyticus but possessed an inhibitory effect on proteases under a wide range of temperature conditions. In addition, in vitro binding assays and molecular docking results indicated that NdCrus1 had a strong binding capacity with chitin. These results provide new insights into crustins in the life activities of N. denticulata sinensis and provide references for studying antibacterial activity characteristics and mechanisms in other crustaceans.http://www.sciencedirect.com/science/article/pii/S2950311625000321CrustinInvertebrate immunityNeocaridina denticulata sinensisWAP domain |
| spellingShingle | Dandan Feng Zhu Zhu Shangpeng Wang Yangcan Gao Yingwen Li Yuying Sun Jiquan Zhang A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis Comparative Immunology Reports Crustin Invertebrate immunity Neocaridina denticulata sinensis WAP domain |
| title | A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis |
| title_full | A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis |
| title_fullStr | A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis |
| title_full_unstemmed | A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis |
| title_short | A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis |
| title_sort | type i crustin with an inhibitory effect on proteases and strong binding capacity to chitin from neocaridina denticulata sinensis |
| topic | Crustin Invertebrate immunity Neocaridina denticulata sinensis WAP domain |
| url | http://www.sciencedirect.com/science/article/pii/S2950311625000321 |
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