A Centipede Toxin Family Defines an Ancient Class of CSαβ Defensins
journal contributionposted on 06.01.2021, 05:29 by Thomas S Dash, Thomas ShafeeThomas Shafee, Peta J Harvey, Chuchu Zhang, Steve Peigneur, Jennifer R Deuis, Irina Vetter, Jan Tytgat, Marilyn AndersonMarilyn Anderson, David J Craik, Thomas Durek, Eivind AB Undheim
© 2018 Elsevier Ltd
Disulfide-rich peptides (DRPs) play many important physiological roles, and can be extremely taxonomically widespread. Here, Dash et al. show that a diverse centipede toxin family belongs to one of the most widespread DRP folds known, the cysteine-stabilized α/β fold, but that it represents a unique, ancient form of this fold.
This work was supported by the Australian Research Council (DECRA Fellowship grant number DE160101142 and Discovery Project grant number DP160104025 to E.A.B.U.). J.T. was supported by grant CELSA/17/047 - BOF/ISP. We thank Prof. David Julius, University of California, San Francisco, United States, for supporting the contributions of C.Z. Antimicrobial screening was performed by CO-ADD (The Community for Antimicrobial Drug Discovery), funded by the Wellcome Trust (UK) and The University of Queensland (Australia). Phylopic image credits: Frank Forster (Enoplea), Gareth Monger (Pseudoscorpiones, Opiliones), Birgit Lang (Collembola), and Matt Crook (Actinobacteria, Acidobacteria, Bacteroidetes, Chlamydiae, Planctomycetes, Proteobacteria, Verrucomicrobia).
Australian Research Council (DECRA Fellowship) | DE160101142
Australian Research Council | DP160104025
Wellcome Trust (UK)
University of Queensland (Australia)
| CELSA/17/047 - BOF/ISP
Pagination19p. (p. 315-326)
Rights StatementThe Author reserves all moral rights over the deposited text and must be credited if any re-use occurs. Documents deposited in OPAL are the Open Access versions of outputs published elsewhere. Changes resulting from the publishing process may therefore not be reflected in this document. The final published version may be obtained via the publisher’s DOI. Please note that additional copyright and access restrictions may apply to the published version.
Science & TechnologyLife Sciences & BiomedicineBiochemistry & Molecular BiologyBiophysicsCell BiologyDISULFIDE BRIDGESCORPION TOXINSSIGNAL PEPTIDESANIMAL TOXINSPROTEINEVOLUTIONSEQUENCEVENOMSDATABASEMOTIFSCells, CulturedAnimalsXenopus laevisHumansMiceArthropodsDefensinsArthropod VenomsEvolution, MolecularPhylogenyMultigene FamilyModels, MolecularMaleProtein Stability3D structureCSαβ foldNMRcentipededefensindisulfide-rich peptideevolutiontoxinCentipede