Dynamic evolution of venom proteins in squamate reptiles

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Dynamic evolution of venom proteins in squamate reptiles. / Wuster, W.; Casewell, N.R.; Wüster, W.

In: Nature Communications, Vol. 3, 18.09.2012, p. Article number: 1066.

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Wuster, W, Casewell, NR & Wüster, W 2012, 'Dynamic evolution of venom proteins in squamate reptiles', Nature Communications, vol. 3, pp. Article number: 1066. https://doi.org/10.1038/ncomms2065

APA

Wuster, W., Casewell, N. R., & Wüster, W. (2012). Dynamic evolution of venom proteins in squamate reptiles. Nature Communications, 3, Article number: 1066. https://doi.org/10.1038/ncomms2065

CBE

Wuster W, Casewell NR, Wüster W. 2012. Dynamic evolution of venom proteins in squamate reptiles. Nature Communications. 3:Article number: 1066. https://doi.org/10.1038/ncomms2065

MLA

Wuster, W., N.R. Casewell and W. Wüster. "Dynamic evolution of venom proteins in squamate reptiles". Nature Communications. 2012, 3. Article number: 1066. https://doi.org/10.1038/ncomms2065

VancouverVancouver

Wuster W, Casewell NR, Wüster W. Dynamic evolution of venom proteins in squamate reptiles. Nature Communications. 2012 Sep 18;3:Article number: 1066. https://doi.org/10.1038/ncomms2065

Author

Wuster, W. ; Casewell, N.R. ; Wüster, W. / Dynamic evolution of venom proteins in squamate reptiles. In: Nature Communications. 2012 ; Vol. 3. pp. Article number: 1066.

RIS

TY - JOUR

T1 - Dynamic evolution of venom proteins in squamate reptiles

AU - Wuster, W.

AU - Casewell, N.R.

AU - Wüster, W.

PY - 2012/9/18

Y1 - 2012/9/18

N2 - Phylogenetic analyses of toxin gene families have revolutionised our understanding of the origin and evolution of reptile venoms, leading to the current hypothesis that venom evolved once in squamate reptiles. However, because of a lack of homologous squamate non-toxin sequences, these conclusions rely on the implicit assumption that recruitments of protein families into venom are both rare and irreversible. Here we use sequences of homologous non-toxin proteins from two snake species to test these assumptions. Phylogenetic and ancestral-state analyses revealed frequent nesting of 'physiological' proteins within venom toxin clades, suggesting early ancestral recruitment into venom followed by reverse recruitment of toxins back to physiological roles. These results provide evidence that protein recruitment into venoms from physiological functions is not a one-way process, but dynamic, with reversal of function and/or co-expression of toxins in different tissues. This requires a major reassessment of our previous understanding of how animal venoms evolve.

AB - Phylogenetic analyses of toxin gene families have revolutionised our understanding of the origin and evolution of reptile venoms, leading to the current hypothesis that venom evolved once in squamate reptiles. However, because of a lack of homologous squamate non-toxin sequences, these conclusions rely on the implicit assumption that recruitments of protein families into venom are both rare and irreversible. Here we use sequences of homologous non-toxin proteins from two snake species to test these assumptions. Phylogenetic and ancestral-state analyses revealed frequent nesting of 'physiological' proteins within venom toxin clades, suggesting early ancestral recruitment into venom followed by reverse recruitment of toxins back to physiological roles. These results provide evidence that protein recruitment into venoms from physiological functions is not a one-way process, but dynamic, with reversal of function and/or co-expression of toxins in different tissues. This requires a major reassessment of our previous understanding of how animal venoms evolve.

U2 - 10.1038/ncomms2065

DO - 10.1038/ncomms2065

M3 - Article

VL - 3

SP - Article number: 1066

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

ER -