ArticleBMC evolutionary biology2015
Adaptive evolution in the toxicity of a spider's venom enzymes.
Article in BMC evolutionary biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Tetracycline reprograms inflammatory and regenerative signaling pathways in human keratinocytes exposed toFrontiers in pharmacology · 2026Article
- Exploring Spiders Without Venom as New Sources of Peptidase Inhibitors.International journal of molecular sciences · 2025Article
- Differential Cellular Responses to Class I and II Sphingomyelinase D: Unraveling the Mechanisms ofInternational journal of molecular sciences · 2025Article
- Discovery of broadly-neutralizing antibodies against brown recluse spider and Gadim scorpion sphingomyelinases using consensus toxins as antigens.Protein science : a publication of the Protein Society · 2024Article
- Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the ScorpionToxins · 2023Article
- Digestive enzymes and sphingomyelinase D in spiders without venom (Uloboridae).Scientific reports · 2023Article
- Sphingomyelinase D Activity inToxins · 2021Article
- Tick-Borne Flavivirus Inhibits Sphingomyelinase (Frontiers in cellular and infection microbiology · 2020Article
- Article
- Population Genomic Analysis of a Pitviper Reveals Microevolutionary Forces Underlying Venom Chemistry.Genome biology and evolution · 2017Article
- Erratum: Adaptive evolution in the toxicity of a spider's venom enzymes.BMC evolutionary biology · 2016Article
- Sphingomyelinase D from Loxosceles laeta Venom Induces the Expression of MMP7 in Human Keratinocytes: Contribution to Dermonecrosis.PloS one · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSphingomyelinase D is the main toxin present in the venom of Loxosceles spiders. Several isoforms present in these venoms can be structurally classified in two groups. Class I Sphingomyelinase D contains a single disulphide bridge and variable loop. Class II Sphingomyelinase D presents an additional intrachain disulphide bridge that links a flexible loop with a catalytic loop. These classes exhibit differences in their toxic potential. In this paper we address the distribution of the structural classes of SMase D within and among species of spiders and also their evolutionary origin by means of phylogenetic analyses. We also conducted tests to assess the action of natural selection in their evolution combined to structural modelling of the affected sites.
resultsThe majority of the Class I enzymes belong to the same clade, which indicates a recent evolution from a single common ancestor. Positively selected sites are located on the catalytic interface, which contributes to a distinct surface charge distribution between the classes. Sites that may prevent the formation of an additional bridge were found in Class I enzymes.
conclusionsThe evolution of Sphingomyelinase D has been driven by natural selection toward an increase in noxiousness, and this might help explain the toxic variation between classes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.