Structural Venomics Reveals Evolution of a Complex Venom by Duplication and Diversification of an Ancient Peptide-Encoding Gene
Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene Sandy S. Pinedaa,b,1,2,3,4, Yanni K.-Y. China,c,1, Eivind A. B. Undheimc,d,e, Sebastian Senffa, Mehdi Moblic, Claire Daulyf, Pierre Escoubasg, Graham M. Nicholsonh, Quentin Kaasa, Shaodong Guoa, Volker Herziga,5, John S. Mattickb,6, and Glenn F. Kinga,2 aInstitute for Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072, Australia; bGarvan-Weizmann Centre for Cellular Genomics, Garvan Institute of Medical Research, Darlinghurst, Sydney, NSW 2010, Australia; cCentre for Advanced Imaging, The University of Queensland, St Lucia, QLD 4072, Australia; dCentre for Biodiversity Dynamics, Department of Biology, Norwegian University of Science and Technology, 7491 Trondheim, Norway; eCentre for Ecological & Evolutionary Synthesis, Department of Biosciences, University of Oslo, 0316 Oslo, Norway; fThermo Fisher Scientific, 91941 Courtaboeuf Cedex, France; gUniversity of Nice Sophia Antipolis, 06000 Nice, France; and hSchool of Life Sciences, University of Technology Sydney, Broadway, NSW 2007, Australia Edited by Adriaan Bax, National Institutes of Health, Bethesda, MD, and approved March 18, 2020 (received for review August 21, 2019) Spiders are one of the most successful venomous animals, with N-terminal strand is sometimes present (12). The cystine knot more than 48,000 described species. Most spider venoms are comprises a “ring” formed by two disulfide bonds and the in- dominated by cysteine-rich peptides with a diverse range of phar- tervening sections of the peptide backbone, with a third disulfide macological activities. Some spider venoms contain thousands of piercing the ring to create a pseudoknot (11).
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