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Exploration of Toxins from a Marine Annelid

2024-02-16Artigo científico Acesso aberto
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dc.contributor.authorRodrigo, Ana P.
dc.contributor.authorMoutinho Cabral, Inês
dc.contributor.authorAlexandre, António
dc.contributor.authorCosta, Pedro M.
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionDCV - Departamento de Ciências da Vida
dc.contributor.pblMDPI - Multidisciplinary Digital Publishing Institute
dc.date.accessioned2024-04-27T00:09:15Z
dc.date.available2024-04-27T00:09:15Z
dc.date.issued2024-02-16
dc.descriptionThe authors acknowledge the Portuguese Foundation for Science and Technology (FCT) for the grant 2022.00252.CEECIND to A.P.R., the grant 2022.11150.BD to I.M.C., the funding of the WormALL project (PTDC/BTA-BTA/28650/2017), and for supporting the Applied Molecular Biosciences Unit—UCIBIO (UIDP/04378/2020 and UIDB/04378/2020) and the Associate Laboratory Institute for Health and Bioeconomy—i4HB (LA/P/0140/2020). The authors also acknowledge Fundo Azul for co-financing the MARVEN project (FA_05_2017_007). Publisher Copyright: © 2024 by the authors.
dc.description.abstractProteinaceous toxins are peptides or proteins that hold great biotechnological value, evidenced by their ecological role, whether as defense or predation mechanisms. Bioprospecting using bioinformatics and omics may render screening for novel bioactives more expeditious, especially considering the immense diversity of toxin-secreting marine organisms. Eulalia sp. (Annelida: Phyllodocidae), a toxin bearing marine annelid, was recently shown to secrete cysteine-rich protein (Crisp) toxins (hitherto referred to as ‘phyllotoxins’) that can immobilize its prey. By analyzing and validating transcriptomic data, we narrowed the list of isolated full coding sequences of transcripts of the most abundant toxins or accompanying bioactives secreted by the species (the phyllotoxin Crisp, hyaluronidase, serine protease, and peptidases M12A, M13, and M12B). Through homology matching with human proteins, the biotechnological potential of the marine annelid’s toxins and related proteins was tentatively associated with coagulative and anti-inflammatory responses for the peptidases PepM12A, SePr, PepM12B, and PepM13, and with the neurotoxic activity of Crisp, and finally, hyaluronidase was inferred to bear properties of an permeabilizing agent. The in silico analysis succeeded by validation by PCR and Sanger sequencing enabled us to retrieve cDNAs can may be used for the heterologous expression of these toxins.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent19
dc.format.extent9947059
dc.identifier.doi10.3390/ani14040635
dc.identifier.issn2076-2615
dc.identifier.otherPURE: 87469385
dc.identifier.otherPURE UUID: fa2d0cee-eadd-476b-922d-9769b3450f29
dc.identifier.otherScopus: 85186953310
dc.identifier.otherWOS: 001172053500001
dc.identifier.otherPubMed: 38396603
dc.identifier.otherPubMedCentral: PMC10885894
dc.identifier.urihttp://hdl.handle.net/10362/166671
dc.identifier.urlhttps://www.scopus.com/pages/publications/85186953310
dc.language.isoeng
dc.peerreviewedyes
dc.relationFunding Information: info:eu-repo/grantAgreement/FCT/CEEC IND5ed/2022.00252.CEECIND%2FCP1725%2FCT0006/PT
dc.relationinfo:eu-repo/grantAgreement/FCT//2022.11150.BD/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBTA-BTA%2F28650%2F2017/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
dc.relationApplied Molecular Biosciences Unit
dc.relationApplied Molecular Biosciences Unit
dc.relationInstitute for Health and Bioeconomy
dc.subjectbioprospecting
dc.subjectbiotechnology
dc.subjecthomology matching
dc.subjectin silico analysis
dc.subjectmarine invertebrates
dc.subjecttoxins
dc.subjectAnimal Science and Zoology
dc.subjectGeneral Veterinary
dc.subjectSDG 14 - Life Below Water
dc.titleExploration of Toxins from a Marine Anneliden
dc.title.subtitleAn Analysis of Phyllotoxins and Accompanying Bioactivesen
dc.typejournal article
degois.publication.issue4
degois.publication.titleAnimals
degois.publication.volume14
dspace.entity.typePublication
oaire.awardNumber2022.11150.BD
oaire.awardNumberPTDC/BTA-BTA/28650/2017
oaire.awardNumberUIDP/04378/2020
oaire.awardNumberUIDB/04378/2020
oaire.awardNumberLA/P/0140/2020
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleApplied Molecular Biosciences Unit
oaire.awardTitleInstitute for Health and Bioeconomy
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//2022.11150.BD/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBTA-BTA%2F28650%2F2017/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04378%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/LA%2FP%2F0140%2F2020/PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
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project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
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