Unravelling the antifungal property of a type I crustin from Scylla olivacea: Membrane disruption and ROS generation as modes of action.
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| Format: | Artículo científico |
| Language: | en |
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Fish & shellfish immunology
2025
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| author | Neelima, S Anju, M V Archana, K Anooja, V V Athira, P P Revathy, M R Mohan, Anjali S Kesavan, Dhanya Philip, Rosamma |
| author_facet | Neelima, S Anju, M V Archana, K Anooja, V V Athira, P P Revathy, M R Mohan, Anjali S Kesavan, Dhanya Philip, Rosamma Neelima, S Anju, M V Archana, K Anooja, V V Athira, P P Revathy, M R Mohan, Anjali S Kesavan, Dhanya Philip, Rosamma |
| collection | PubMed - marine biology |
| contents | Unravelling the antifungal property of a type I crustin from Scylla olivacea: Membrane disruption and ROS generation as modes of action. Neelima, S Anju, M V Archana, K Anooja, V V Athira, P P Revathy, M R Mohan, Anjali S Kesavan, Dhanya Philip, Rosamma Antifungal Agents Animals Reactive Oxygen Species Antimicrobial Cationic Peptides Arthropod Proteins Brachyura Cell Membrane Amino Acid Sequence Crustins, among the earliest families of gene-encoded antimicrobial peptides (AMPs) identified in crustaceans, are disulfide-rich peptides (6-22 kDa) characterized by a conserved Whey Acidic Protein (WAP) domain at the C-terminal end. This domain features a disulfide core formed by eight highly conserved cysteines. Functionally, crustins exhibit diverse biological roles. In this study, we demonstrate the in vitro antifungal efficacy and explore the mechanisms of action of So-Crustin, a Type-I crustin isoform derived from the Orange mud-crab Scylla olivacea. The recombinant peptide displayed potent antifungal activity, marked by rapid, membrane-targeted disruptions as nanoscale pores, |
| format | Artículo científico |
| id | pubmed_40651732 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Fish & shellfish immunology |
| record_format | pubmed |
| spellingShingle | Unravelling the antifungal property of a type I crustin from Scylla olivacea: Membrane disruption and ROS generation as modes of action. Neelima, S Anju, M V Archana, K Anooja, V V Athira, P P Revathy, M R Mohan, Anjali S Kesavan, Dhanya Philip, Rosamma Antifungal Agents Animals Reactive Oxygen Species Antimicrobial Cationic Peptides Arthropod Proteins Brachyura Cell Membrane Amino Acid Sequence Unravelling the antifungal property of a type I crustin from Scylla olivacea: Membrane disruption and ROS generation as modes of action. Neelima, S Anju, M V Archana, K Anooja, V V Athira, P P Revathy, M R Mohan, Anjali S Kesavan, Dhanya Philip, Rosamma Antifungal Agents Animals Reactive Oxygen Species Antimicrobial Cationic Peptides Arthropod Proteins Brachyura Cell Membrane Amino Acid Sequence Crustins, among the earliest families of gene-encoded antimicrobial peptides (AMPs) identified in crustaceans, are disulfide-rich peptides (6-22 kDa) characterized by a conserved Whey Acidic Protein (WAP) domain at the C-terminal end. This domain features a disulfide core formed by eight highly conserved cysteines. Functionally, crustins exhibit diverse biological roles. In this study, we demonstrate the in vitro antifungal efficacy and explore the mechanisms of action of So-Crustin, a Type-I crustin isoform derived from the Orange mud-crab Scylla olivacea. The recombinant peptide displayed potent antifungal activity, marked by rapid, membrane-targeted disruptions as nanoscale pores, |
| title | Unravelling the antifungal property of a type I crustin from Scylla olivacea: Membrane disruption and ROS generation as modes of action. |
| topic | Antifungal Agents Animals Reactive Oxygen Species Antimicrobial Cationic Peptides Arthropod Proteins Brachyura Cell Membrane Amino Acid Sequence |
| url | https://pubmed.ncbi.nlm.nih.gov/40651732/ |