Biology subjects

Dresler, J.

Publications and source records attributed to Dresler, J..

3 recordsLinked to original sources

bioRxiv2025

Transcriptomic assessment of the Black Judaicus scorpion (Hottentotta judaicus) toxin arsenal and its potential bioeconomic value

Scorpion venoms are likewise a medical burden as well as a source of novel bioresources. Despite their important dual role, the venoms of most scorpion species remain under- or unstudied. Among these is the venom of the Black Judaicus scorpion, Hottentotta judaicus (Simon, 1872), a common yet neglected species native to the Middle East. Here, we employ venom gland transcriptomics to investigate its toxin-encoding precursor profile to gain insight into its toxin repertoire. The venom was found to be composed primarily of various short scorpion toxins, long scorpion toxins from the 3 C-C as well as the 4 C-C type, and enzymatic components. Minor components include, defensins and putative antimicrobial peptides. Several identified toxins show similarity to known neurotoxins from lethal buthids or to toxins with translational value in biomedicine, agriculture, and industrial production, thus rendering H. judaicus both, a potential health concern and source of novel bioresources. Our work provides an extended perspective on the venom profile of this species and represents a basis for future follow-up studies.

zoology↗

bioRxiv2025

Convergent evolutionary adaption of spider venom from predation to defense

Most spiders deploy paralytic venom for prey capture, but adults of the yellow-sac spider (Cheiracanthium punctorium) instead produce a predominantly defensive venom to safeguard their offspring. Here, we characterized the molecular repertoire of C. punctorium venom to shed light on its evolutionary history. Unlike venom in other spiders, C. punctorium venom mostly comprises neurotoxic double-domain neurotoxin 19 family (CSTX) peptides and enzymes, such as phospholipase A2 (PLA2). Comparative venomics in four spiders representing two infraorders showed that CSTXs arose following the mygalomorph- araneomorph split [~]300 mya by means of ancestral gene duplication and functional specialization. A gene fusion event then merged CSTXs from two distinct clades to form the double-domain toxin. PLA2 proteins were convergently recruited to C. punctorium to fulfil a defensive function and are strikingly similar to proalgesic PLA2 proteins in bee venom. These complex, multimodal molecular innovations in venom systems highlight natures tendency to use the same molecular solutions for similar ecological challenges across diverse animal lineages.

zoology↗

bioRxiv2024

Enlighting the toxinological dark matter of spider venom enzymes

Spiders produce highly adapted venoms featuring a complex mixture of biomolecules used mainly for hunting and defense. The most prominent components are peptidic neurotoxins, which have been the focus of research and drug development, whereas venom enzymes have been largely neglected. Nevertheless, investigation of venom enzymes not only reveals insights into their biological functions, but also provides templates for future industrial applications. Here we compared spider venom enzymes contained in the VenomZone database and in other publicly available proteo-transcriptomic datasets. We found extensive discrepancies between these sources, revealing a previously unrecognized abundance and diversity of venom enzymes. Furthermore, we assigned the reported enzymes to cellular processes and known venom functions, including toxicity, prey pre-digestion, venom preservation, venom component activation, and venom spreading factors. Our study reveals a gap between databases and publications in terms of enzyme coverage which impedes development of new applications based on the rich and diverse spectrum of enzymes contained in spider venom.

biochemistry↗