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"beyond Primary Sequence" - Proteomic Data Reveal Complex Toxins in Cnidarian Venoms

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"beyond Primary Sequence" - Proteomic Data Reveal Complex Toxins in Cnidarian Venoms. / Jaimes-Becerra, Adrian; Gacesa, Ranko; Doonan, Liam B.; Hartigan, Ashlie; Marques, Antonio C.; Okamura, Beth; Long, Paul F.

In: INTEGRATIVE AND COMPARATIVE BIOLOGY, Vol. 59, No. 4, 01.10.2019, p. 777-785.

Research output: Contribution to journalArticle

Harvard

Jaimes-Becerra, A, Gacesa, R, Doonan, LB, Hartigan, A, Marques, AC, Okamura, B & Long, PF 2019, '"beyond Primary Sequence" - Proteomic Data Reveal Complex Toxins in Cnidarian Venoms', INTEGRATIVE AND COMPARATIVE BIOLOGY, vol. 59, no. 4, pp. 777-785. https://doi.org/10.1093/icb/icz106

APA

Jaimes-Becerra, A., Gacesa, R., Doonan, L. B., Hartigan, A., Marques, A. C., Okamura, B., & Long, P. F. (2019). "beyond Primary Sequence" - Proteomic Data Reveal Complex Toxins in Cnidarian Venoms. INTEGRATIVE AND COMPARATIVE BIOLOGY, 59(4), 777-785. https://doi.org/10.1093/icb/icz106

Vancouver

Jaimes-Becerra A, Gacesa R, Doonan LB, Hartigan A, Marques AC, Okamura B et al. "beyond Primary Sequence" - Proteomic Data Reveal Complex Toxins in Cnidarian Venoms. INTEGRATIVE AND COMPARATIVE BIOLOGY. 2019 Oct 1;59(4):777-785. https://doi.org/10.1093/icb/icz106

Author

Jaimes-Becerra, Adrian ; Gacesa, Ranko ; Doonan, Liam B. ; Hartigan, Ashlie ; Marques, Antonio C. ; Okamura, Beth ; Long, Paul F. / "beyond Primary Sequence" - Proteomic Data Reveal Complex Toxins in Cnidarian Venoms. In: INTEGRATIVE AND COMPARATIVE BIOLOGY. 2019 ; Vol. 59, No. 4. pp. 777-785.

Bibtex Download

@article{4987131c9f664464995444ea0a58e155,
title = "{"}beyond Primary Sequence{"} - Proteomic Data Reveal Complex Toxins in Cnidarian Venoms",
abstract = "Venomous animals can deploy toxins for both predation and defense. These dual functions of toxins might be expected to promote the evolution of new venoms and alteration of their composition. Cnidarians are the most ancient venomous animals but our present understanding of their venom diversity is compromised by poor taxon sampling. New proteomic data were therefore generated to characterize toxins in venoms of a staurozoan, a hydrozoan, and an anthozoan. We then used a novel clustering approach to compare venom diversity in cnidarians to other venomous animals. Comparison of the presence or absence of 32 toxin protein families indicated venom composition did not vary widely among the 11 cnidarian species studied. Unsupervised clustering of toxin peptide sequences suggested that toxin composition of cnidarian venoms is just as complex as that in many venomous bilaterians, including marine snakes. The adaptive significance of maintaining a complex and relatively invariant venom remains unclear. Future study of cnidarian venom diversity, venom variation with nematocyst types and in different body regions are required to better understand venom evolution.",
author = "Adrian Jaimes-Becerra and Ranko Gacesa and Doonan, {Liam B.} and Ashlie Hartigan and Marques, {Antonio C.} and Beth Okamura and Long, {Paul F.}",
year = "2019",
month = "10",
day = "1",
doi = "10.1093/icb/icz106",
language = "English",
volume = "59",
pages = "777--785",
journal = "INTEGRATIVE AND COMPARATIVE BIOLOGY",
issn = "1450-7063",
publisher = "Oxford University Press",
number = "4",

}

RIS (suitable for import to EndNote) Download

TY - JOUR

T1 - "beyond Primary Sequence" - Proteomic Data Reveal Complex Toxins in Cnidarian Venoms

AU - Jaimes-Becerra, Adrian

AU - Gacesa, Ranko

AU - Doonan, Liam B.

AU - Hartigan, Ashlie

AU - Marques, Antonio C.

AU - Okamura, Beth

AU - Long, Paul F.

PY - 2019/10/1

Y1 - 2019/10/1

N2 - Venomous animals can deploy toxins for both predation and defense. These dual functions of toxins might be expected to promote the evolution of new venoms and alteration of their composition. Cnidarians are the most ancient venomous animals but our present understanding of their venom diversity is compromised by poor taxon sampling. New proteomic data were therefore generated to characterize toxins in venoms of a staurozoan, a hydrozoan, and an anthozoan. We then used a novel clustering approach to compare venom diversity in cnidarians to other venomous animals. Comparison of the presence or absence of 32 toxin protein families indicated venom composition did not vary widely among the 11 cnidarian species studied. Unsupervised clustering of toxin peptide sequences suggested that toxin composition of cnidarian venoms is just as complex as that in many venomous bilaterians, including marine snakes. The adaptive significance of maintaining a complex and relatively invariant venom remains unclear. Future study of cnidarian venom diversity, venom variation with nematocyst types and in different body regions are required to better understand venom evolution.

AB - Venomous animals can deploy toxins for both predation and defense. These dual functions of toxins might be expected to promote the evolution of new venoms and alteration of their composition. Cnidarians are the most ancient venomous animals but our present understanding of their venom diversity is compromised by poor taxon sampling. New proteomic data were therefore generated to characterize toxins in venoms of a staurozoan, a hydrozoan, and an anthozoan. We then used a novel clustering approach to compare venom diversity in cnidarians to other venomous animals. Comparison of the presence or absence of 32 toxin protein families indicated venom composition did not vary widely among the 11 cnidarian species studied. Unsupervised clustering of toxin peptide sequences suggested that toxin composition of cnidarian venoms is just as complex as that in many venomous bilaterians, including marine snakes. The adaptive significance of maintaining a complex and relatively invariant venom remains unclear. Future study of cnidarian venom diversity, venom variation with nematocyst types and in different body regions are required to better understand venom evolution.

UR - http://www.scopus.com/inward/record.url?scp=85073584183&partnerID=8YFLogxK

U2 - 10.1093/icb/icz106

DO - 10.1093/icb/icz106

M3 - Article

C2 - 31225595

AN - SCOPUS:85073584183

VL - 59

SP - 777

EP - 785

JO - INTEGRATIVE AND COMPARATIVE BIOLOGY

JF - INTEGRATIVE AND COMPARATIVE BIOLOGY

SN - 1450-7063

IS - 4

ER -

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