Biology subjects

Herzig, V.

Publications and source records attributed to Herzig, V..

5 recordsLinked to original sources

bioRxiv2026

A Draft Male Genome Assembly of the Slipper Lobster (Thenus australiensis) Reveals an XY System and a Validated Diagnostic Marker for Monosex Aquaculture.

The slipper lobster (Thenus australiensis) is rapidly emerging as a high-potential species for commercial aquaculture. Because females exhibit superior growth characteristics due to less frequent moulting after sexual maturity, developing monosex breeding strategies is highly desirable for industry profitability. However, the lack of genomic resources and early sex-identification tools has hindered this development. Here, we report the first draft male genome assembly for T. australiensis, generated using a combination of whole-genome shotgun sequencing, DArT-seq, and multi-tissue transcriptomics. The curated assembly spans 0.913 Gbp with high functional completeness (93.0% BUSCO), providing a robust repertoire of 30,100 protein-coding genes. Through k-mer subtraction and population-level DArT-seq genotyping, we provide definitive evidence that T. australiensis utilizes an XX/XY sex-determination system. Crucially, by identifying male-specific structural variations within a neo-Y locus, we developed a diagnostic PCR assay targeting a male-exclusive sequence. This 171 bp marker achieved 100% accuracy in phenotypic sex identification across wild-caught populations. Ultimately, these foundational genomic resources, combined with a highly reliable molecular sexing tool, provide the critical framework necessary for early sex sorting, broodstock management, and the commercial advancement of monosex slipper lobster farming. HighlightsO_LIFirst draft genome of slipper lobster (0.913 Gbp) assembled. C_LIO_LIMulti-omics approach confirms an XX/XY sex-determination system. C_LIO_LIDeveloped a 171 bp diagnostic PCR sex marker with 100% accuracy. C_LIO_LIFacilitates early sex sorting for profitable monosex aquaculture. C_LI

genomics↗

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↗

bioRxiv2020

Heterodimeric insecticidal peptide provides new insights into the molecular and functional diversity of ant venoms

Ants use venom for predation, defence and communication, however, the molecular diversity, function and potential applications of ant venom remains understudied compared to other venomous lineages such as arachnids, snakes and cone snails. In this work, we used a multidisciplinary approach that encompassed field work, proteomics, sequencing, chemical synthesis, structural analysis, molecular modelling, stability studies, and a series of in vitro and in vivo bioassays to investigate the molecular diversity of the venom of the Amazonian Pseudomyrmex penetrator ants. We isolated a potent insecticidal heterodimeric peptide {Delta}-pseudomyrmecitoxin-Pp1a ({Delta}-PSDTX-Pp1a) composed of a 27-residue long A-chain and a 33-residue long B-chain crosslinked by two disulfide bonds in an antiparallel orientation. We chemically synthesised {Delta}-PSDTX-Pp1a, its corresponding parallel AA and BB homodimers, and its monomeric chains and demonstrated that {Delta}-PSDTX-Pp1a had the most potent insecticidal effects in blow fly assays (LD50 = 3 nM). Molecular modelling and circular dichroism studies revealed strong alpha-helical features, indicating its cytotoxic effects could derive from membrane disruption, which was further supported by insect cell calcium assays. The native heterodimer was also substantially more stable against proteolytic degradation (t1/2 =13 h) than its homodimers or monomers (t1/2 <20 min), indicating an evolutionary advantage of the more complex structure. The proteomic analysis of Pseudomyrmex penetrator venom and in-depth characterisation of {Delta}-PSDTX-Pp1a provide novel insights in the structural complexity of ant venom, and further exemplifies how nature exploits disulfide-bond formation and dimerization to gain an evolutionary advantage via improved stability; a concept that is also highly relevant for the design and development of peptide therapeutics, molecular probes and bioinsecticides.

pharmacology and toxicology↗