TY - JOUR
T1 - Exploration of Toxins from a Marine Annelid
T2 - An Analysis of Phyllotoxins and Accompanying Bioactives
AU - Rodrigo, Ana P.
AU - Moutinho Cabral, Inês
AU - Alexandre, António
AU - Costa, Pedro M.
N1 - Funding Information:
info:eu-repo/grantAgreement/FCT/CEEC IND5ed/2022.00252.CEECIND%2FCP1725%2FCT0006/PT#
info:eu-repo/grantAgreement/FCT//2022.11150.BD/PT#
info:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBTA-BTA%2F28650%2F2017/PT#
info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F04378%2F2020/PT#
info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F04378%2F2020/PT#
info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/LA%2FP%2F0140%2F2020/PT#
The 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.
PY - 2024/2/16
Y1 - 2024/2/16
N2 - Proteinaceous 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.
AB - Proteinaceous 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.
KW - bioprospecting
KW - biotechnology
KW - homology matching
KW - in silico analysis
KW - marine invertebrates
KW - toxins
UR - http://www.scopus.com/inward/record.url?scp=85186953310&partnerID=8YFLogxK
U2 - 10.3390/ani14040635
DO - 10.3390/ani14040635
M3 - Article
C2 - 38396603
AN - SCOPUS:85186953310
SN - 2076-2615
VL - 14
JO - Animals
JF - Animals
IS - 4
M1 - 635
ER -