Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene.

Pineda, SS; Chin, YK-Y; Undheim, EAB; Senff, S; Mobli, M; Dauly, C; Escoubas, P; Nicholson, GM; Kaas, Q; Guo, S; Herzig, V; Mattick, JS; King, GF

Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene.

Pineda, SS Chin, YK-Y Undheim, EAB Senff, S Mobli, M Dauly, C Escoubas, P Nicholson, GM Kaas, Q Guo, S Herzig, V Mattick, JS King, GF

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Publisher:: NATL ACAD SCIENCES
Publication Type:: Journal Article
Citation:: Proceedings of the National Academy of Sciences of the United States of America, 2020, 117, (21), pp. 11399-11408
Issue Date:: 2020-05-12

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Field	Value	Language
dc.contributor.author	Pineda, SS
dc.contributor.author	Chin, YK-Y
dc.contributor.author	Undheim, EAB
dc.contributor.author	Senff, S
dc.contributor.author	Mobli, M
dc.contributor.author	Dauly, C
dc.contributor.author	Escoubas, P
dc.contributor.author	Nicholson, GM
dc.contributor.author	Kaas, Q
dc.contributor.author	Guo, S
dc.contributor.author	Herzig, V
dc.contributor.author	Mattick, JS
dc.contributor.author	King, GF
dc.date.accessioned	2020-10-22T05:24:26Z
dc.date.available	2020-10-22T05:24:26Z
dc.date.issued	2020-05-12
dc.identifier.citation	Proceedings of the National Academy of Sciences of the United States of America, 2020, 117, (21), pp. 11399-11408
dc.identifier.issn	0027-8424
dc.identifier.issn	1091-6490
dc.identifier.uri	http://hdl.handle.net/10453/143474
dc.description.abstract	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.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	NATL ACAD SCIENCES
dc.relation.ispartof	Proceedings of the National Academy of Sciences of the United States of America
dc.relation.isbasedon	10.1073/pnas.1914536117
dc.rights	info:eu-repo/semantics/restrictedAccess
dc.subject.mesh	Animals
dc.subject.mesh	Spiders
dc.subject.mesh	Diptera
dc.subject.mesh	Disulfides
dc.subject.mesh	Peptides
dc.subject.mesh	Spider Venoms
dc.subject.mesh	Gene Expression Profiling
dc.subject.mesh	Proteomics
dc.subject.mesh	Evolution, Molecular
dc.subject.mesh	Phylogeny
dc.subject.mesh	Protein Conformation
dc.subject.mesh	Australia
dc.subject.mesh	Female
dc.subject.mesh	Mass Spectrometry
dc.subject.mesh	Arthropod Proteins
dc.subject.mesh	Animals
dc.subject.mesh	Spiders
dc.subject.mesh	Diptera
dc.subject.mesh	Disulfides
dc.subject.mesh	Peptides
dc.subject.mesh	Spider Venoms
dc.subject.mesh	Gene Expression Profiling
dc.subject.mesh	Proteomics
dc.subject.mesh	Evolution, Molecular
dc.subject.mesh	Phylogeny
dc.subject.mesh	Protein Conformation
dc.subject.mesh	Australia
dc.subject.mesh	Female
dc.subject.mesh	Mass Spectrometry
dc.subject.mesh	Arthropod Proteins
dc.subject.mesh	Animals
dc.subject.mesh	Arthropod Proteins
dc.subject.mesh	Australia
dc.subject.mesh	Diptera
dc.subject.mesh	Disulfides
dc.subject.mesh	Evolution, Molecular
dc.subject.mesh	Female
dc.subject.mesh	Gene Expression Profiling
dc.subject.mesh	Mass Spectrometry
dc.subject.mesh	Peptides
dc.subject.mesh	Phylogeny
dc.subject.mesh	Protein Conformation
dc.subject.mesh	Proteomics
dc.subject.mesh	Spider Venoms
dc.subject.mesh	Spiders
dc.title	Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene.
dc.type	Journal Article
utslib.citation.volume	117
utslib.location.activity	United States
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
pubs.organisational-group	/University of Technology Sydney
utslib.copyright.status	closed_access	*
pubs.consider-herdc	false
dc.date.updated	2020-10-22T05:23:54Z
pubs.issue	21
pubs.publication-status	Published
pubs.volume	117
utslib.citation.issue	21

Abstract:

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.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/143474