Your browser doesn't support javascript.
loading
Jellyfish Venom Peptides Targeting Human Potassium Channels Identified through Ligand Screening: Morphometric and Molecular Identification of the Species and Antibiotic Potential.
Edirisinghe, Edirisinghe Arachchige Hashini Wasthala; Athukorala, Buddhima Nirmani; Perera, Minoli; Abeywardana, Bothunga Arachchige Shamali Dilhara; Sigera, Polgahawattage Sachini Tarushika; Eranga, Pasindu; Theekshana, Kavindu Dinuhara; Boudjelal, Mohamad; Ali, Rizwan; Peiris, Dinithi Champika.
Afiliación
  • Edirisinghe EAHW; Department of Zoology, Faculty of Applied Sciences, University of Sri Jayewardenepura, Nugegoda 10250, Sri Lanka.
  • Athukorala BN; Department of Zoology, Faculty of Applied Sciences, University of Sri Jayewardenepura, Nugegoda 10250, Sri Lanka.
  • Perera M; Department of Zoology, Faculty of Applied Sciences, University of Sri Jayewardenepura, Nugegoda 10250, Sri Lanka.
  • Abeywardana BASD; Department of Zoology, Faculty of Applied Sciences, University of Sri Jayewardenepura, Nugegoda 10250, Sri Lanka.
  • Sigera PST; Genetics and Molecular Biology Unit, Faculty of Applied Sciences, University of Sri Jayewardenepura, Nugegoda 10250, Sri Lanka.
  • Eranga P; Department of Zoology, Faculty of Applied Sciences, University of Sri Jayewardenepura, Nugegoda 10250, Sri Lanka.
  • Theekshana KD; Department of Zoology, Faculty of Applied Sciences, University of Sri Jayewardenepura, Nugegoda 10250, Sri Lanka.
  • Boudjelal M; King Abdullah International Medical Research Center (KAIMRC), Medical Research Core Facility, and Platforms (MRCFP), King Saud bin Abdulaziz University for Health Sciences (KSAU-HS), Ministry of National Guard Health Affairs (MNGHA), Riyadh 11481, Saudi Arabia.
  • Ali R; King Abdullah International Medical Research Center (KAIMRC), Medical Research Core Facility, and Platforms (MRCFP), King Saud bin Abdulaziz University for Health Sciences (KSAU-HS), Ministry of National Guard Health Affairs (MNGHA), Riyadh 11481, Saudi Arabia.
  • Peiris DC; Department of Zoology, Faculty of Applied Sciences, University of Sri Jayewardenepura, Nugegoda 10250, Sri Lanka.
Mar Drugs ; 22(8)2024 Jul 24.
Article en En | MEDLINE | ID: mdl-39195449
ABSTRACT
The relative lack of marine venom could be attributed to the difficulty in dealing with venomous marine animals. Moreover, the venom of marine animals consists of various bioactive molecules, many of which are proteins with unique properties. In this study, we investigated the potential toxic proteins of jellyfish collected for ligand screening to understand the mechanism of the toxic effects of jellyfish. Since taxonomic identification is problematic due to the lack of proper keys, we conducted morphological and molecular mitochondrial DNA sequencing from COI and ITS regions. The venom extract from nematocysts found along the bell margins was used for protein characterization using SDS-gel electrophoresis and nano-liquid chromatography-tandem mass spectrometry. Ligand screening for the most potent toxin and antibacterial and cytotoxicity assays were carried out. The phylogenetic tree showed distinct clustering from other Catostylus sp. The proteomic analysis revealed venom with many bioactive proteins. Only 13 venom proteins were identified with molecular weights ranging from 4318 to 184,923 Da, exhibiting the venom's complexity. The overall toxin protein composition of Catostylus sp. venom was dominated by potassium channel toxin alpha-KTx. Molecular docking of toxin alpha-KTx 1.13 revealed high specificity towards the human voltage-gated potassium channel Kv3 with a high fitness score and a minimum energy barrier of -17.9 kcal/mol. Disc diffusion and cytotoxicity assays revealed potent antibacterial activity against Klebsiella pneumoniae with no cytotoxicity. Further studies on detailed characterization and therapeutic potentials are warranted.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Venenos de Cnidarios / Simulación del Acoplamiento Molecular / Antibacterianos Límite: Animals / Humans Idioma: En Revista: Mar Drugs Asunto de la revista: BIOLOGIA / FARMACOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Sri Lanka Pais de publicación: Suiza
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Péptidos / Venenos de Cnidarios / Simulación del Acoplamiento Molecular / Antibacterianos Límite: Animals / Humans Idioma: En Revista: Mar Drugs Asunto de la revista: BIOLOGIA / FARMACOLOGIA Año: 2024 Tipo del documento: Article País de afiliación: Sri Lanka Pais de publicación: Suiza