Dataset Information

Evaluating the potential for evolutionary mismatch in Batesian mimics: A case study in the endangered smooth snake (Coronella austriaca).

ABSTRACT: Many harmless organisms gain a survival advantage by mimicking venomous species. This is the case of the endangered smooth snake (Coronella austriaca), which mimics venomous vipers. Although this may protect the smooth snake against most of its natural predators, it may render them at greater risk of mortality from humans, who are more inclined to kill species, such as vipers, that they consider dangerous. This may cause an evolutionary mismatch, whereby humans may counteract the natural advantage of mimicry. We explore this possibility of evaluating the willingness of humans to kill smooth snakes versus the adder (Vipera berus), as well as their ability to discern them in the Åland Islands. Our results show that, even when respondents did not wish to kill the smooth snakes, these were often mistaken for adders, which they were willing to kill. Altogether, viper mimicry brought about a 2.3-fold increase in the likelihood of smooth snakes being killed upon human encounter. These results open up the possibility that naturally selected mimicry can pose a threat to endangered snakes in human-influenced habitats. We discuss the potential for this to be the case, and highlight the importance of protecting entire mimicry complexes, rather than single species, when the endangered species is a mimic.

SUBMITTER: Valkonen JK

PROVIDER: S-EPMC6183469 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Evaluating the potential for evolutionary mismatch in Batesian mimics: A case study in the endangered smooth snake (<i>Coronella austriaca</i>).

Valkonen Janne K JK Mäkelä Anni A Mappes Johanna J López-Sepulcre Andrés A

Evolutionary applications 20180811 9

Many harmless organisms gain a survival advantage by mimicking venomous species. This is the case of the endangered smooth snake (<i>Coronella austriaca</i>), which mimics venomous vipers. Although this may protect the smooth snake against most of its natural predators, it may render them at greater risk of mortality from humans, who are more inclined to kill species, such as vipers, that they consider dangerous. This may cause an evolutionary mismatch, whereby humans may counteract the natural ...[more]

PMID: 30344623

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Project description:Peptide mimics that display amino acid side-chains on semi-rigid scaffolds (not peptide polyamides) can be referred to as minimalist mimics. Accessible conformations of these scaffolds may overlay with secondary structures giving, for example, "minimalist helical mimics". It is difficult for researchers who want to apply minimalist mimics to decide which one to use because there is no widely accepted protocol for calibrating how closely these compounds mimic secondary structures. Moreover, it is also difficult for potential practitioners to evaluate which ideal minimalist helical mimics are preferred for a particular set of side-chains. For instance, what mimic presents i, i + 4, i + 7 side-chains in orientations that best resemble an ideal ?-helix, and is a different mimic required for a i, i + 3, i + 7 helical combination? This article describes a protocol for fitting each member of an array of accessible scaffold conformations on secondary structures. The protocol involves: (i) use quenched molecular dynamics (QMD) to generate an ensemble consisting of hundreds of accessible, low energy conformers of the mimics; (ii) representation of each of these as a set of C? and C? coordinates corresponding to three amino acid side-chains displayed by the scaffolds; (iii) similar representation of each combination of three side-chains in each ideal secondary structure as a set of C? and C? coordinates corresponding to three amino acid side-chains displayed by the scaffolds; and, (iv) overlay C? and C? coordinates of all the conformers on all the sets of side-chain "triads" in the ideal secondary structures and express the goodness of fit in terms of root mean squared deviation (RMSD, Å) for each overlay. We refer to this process as Exploring Key Orientations on Secondary structures (EKOS). Application of this procedure reveals the relative bias of a scaffold to overlay on different secondary structures, the "side-chain correspondences" (e.g. i, i + 4, i + 7 or i, i + 3, i + 4) of those overlays, and the energy of this state relative to the minimum located. This protocol was tested on some of the most widely cited minimalist ?-helical mimics (1-8 in the text). The data obtained indicates several of these compounds preferentially exist in conformations that resemble other secondary structures as well as ?-helices, and many of the ?-helical conformations have unexpected side-chain correspondences. These observations imply the featured minimalist mimics have more scope for disrupting PPI interfaces than previously anticipated. Finally, the same simulation method was used to match preferred conformations of minimalist mimics with actual protein/peptide structures at interfaces providing quantitative comparisons of predicted fits of the test mimics at protein-protein interaction sites.

Dataset Information

Evaluating the potential for evolutionary mismatch in Batesian mimics: A case study in the endangered smooth snake (Coronella austriaca).

Publications

Evaluating the potential for evolutionary mismatch in Batesian mimics: A case study in the endangered smooth snake (<i>Coronella austriaca</i>).

Similar Datasets

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