Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene.
proteomics
spider venom
structural venomics
transcriptomics
venom evolution
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
26 05 2020
26 05 2020
Historique:
pubmed:
14
5
2020
medline:
25
8
2020
entrez:
14
5
2020
Statut:
ppublish
Résumé
Spiders are one of the most successful venomous animals, with more than 48,000 described species. Most spider venoms are dominated by cysteine-rich peptides with a diverse range of pharmacological activities. Some spider venoms contain thousands of unique peptides, but little is known about the mechanisms used to generate such complex chemical arsenals. We used an integrated transcriptomic, proteomic, and structural biology approach to demonstrate that the lethal Australian funnel-web spider produces 33 superfamilies of venom peptides and proteins. Twenty-six of the 33 superfamilies are disulfide-rich peptides, and we show that 15 of these are knottins that contribute >90% of the venom proteome. NMR analyses revealed that most of these disulfide-rich peptides are structurally related and range in complexity from simple to highly elaborated knottin domains, as well as double-knot toxins, that likely evolved from a single ancestral toxin gene.
Identifiants
pubmed: 32398368
pii: 1914536117
doi: 10.1073/pnas.1914536117
pmc: PMC7260951
doi:
Substances chimiques
Arthropod Proteins
0
Disulfides
0
Peptides
0
Spider Venoms
0
Banques de données
PDB
['2N6N', '2N6R', '6BA3', '2N8K']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
11399-11408Déclaration de conflit d'intérêts
Competing interest statement: C.D. is affiliated with Thermo Fisher Scientific.
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