ArticleThe journal of venomous animals and toxins including tropical diseases2014
Purification and characterization of a hyaluronidase from venom of the spider Vitalius dubius (Araneae, Theraphosidae).
Article in The journal of venomous animals and toxins including tropical diseases, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 39 citations in OpenAlex.
- From permeation enhancer to therapeutic enabler: Advances, applications, and translational perspectives in hyaluronidase-based drug delivery.Materials today. Bio · 2026Review
- A Hydrolase-Rich Venom Beyond Neurotoxins: Integrative Functional Proteomic and Immunoreactivity Analyses Reveal Novel Peptides in the Amazonian ScorpionInternational journal of molecular sciences · 2026Article
- Pharmacological characterization and nephroprotective potential of venoms from three egyptian scorpion species.Frontiers in pharmacology · 2026Article
- Enzymatic characterization and proteomic profiling of venoms from the medically important Androctonus species.Journal, genetic engineering & biotechnology · 2025Article
- Prospects and challenges of recombinant spider venom enzymes: insights fromFrontiers in bioengineering and biotechnology · 2025Article
- YsHyl8A, an Alkalophilic Cold-Adapted Glycosaminoglycan Lyase Cloned from PathogenicMolecules (Basel, Switzerland) · 2022Article
- Transcriptomic Analysis of the Venom Gland and Enzymatic Characterization of the Venom ofToxins · 2022Article
- Brazilian Theraphosidae: a toxicological point of view.The journal of venomous animals and toxins including tropical diseases · 2021Review
- Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid ScorpionToxins · 2018Article
- Virocidal activity of Egyptian scorpion venoms against hepatitis C virus.Virology journal · 2015Article
- Isolation, N-glycosylations and Function of a Hyaluronidase-Like Enzyme from the Venom of the Spider Cupiennius salei.PloS one · 2015Article
- Arthropod venom Hyaluronidases: biochemical properties and potential applications in medicine and biotechnology.The journal of venomous animals and toxins including tropical diseases · 2015Article
- Pharmacological characterization of venoms from three theraphosid spiders: Poecilotheria regalis, Ceratogyrus darlingi and Brachypelma epicureanum.The journal of venomous animals and toxins including tropical diseases · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundVenom hyaluronidase (Hyase) contributes to the diffusion of venom from the inoculation site. In this work, we purified and characterized Hyase from the venom of Vitalius dubius (Araneae, Theraphosidae), a large theraphosid found in southeastern Brazil. Venom obtained by electrical stimulation of adult male and female V. dubius was initially fractionated by gel filtration on a Superdex® 75 column. Active fractions were pooled and applied to a heparin-sepharose affinity column. The proteins were eluted with a linear NaCl gradient.
resultsActive fractions were pooled and assessed for purity by SDS-PAGE and RP-HPLC. The physicochemical tests included optimum pH, heat stability, presence of isoforms, neutralization by flavonoids and assessment of commercial antivenoms. Hyase was purified and presented a specific activity of 148 turbidity-reducing units (TRU)/mg (venom: 36 TRU/mg; purification factor of ~4). Hyase displayed a molecular mass of 43 kDa by SDS-PAGE. Zymography in hyaluronic-acid-containing gels indicated an absence of enzyme isoforms. The optimum pH was 4-5, with highest activity at 37°C. Hyase was stable up to 60°C; but its activity was lost at higher temperatures and maintained after several freeze-thaw cycles. The NaCl concentration (up to 1 M) did not influence activity. Hyase had greater action towards hyaluronic acid compared to chondroitin sulfate, and was completely neutralized by polyvalent antiarachnid sera, but not by caterpillar, scorpion or snakes antivenoms.
conclusionThe neutralization by arachnid but not scorpion antivenom indicates that this enzyme shares antigenic epitopes with similar enzymes in other spider venoms. The biochemical properties of this Hyase are comparable to others described.
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