Volker Herzig

ORCID: 0000-0003-2514-3983
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About
Contact & Profiles
Research Areas
  • Venomous Animal Envenomation and Studies
  • Insect and Pesticide Research
  • Ion channel regulation and function
  • Nicotinic Acetylcholine Receptors Study
  • Antimicrobial Peptides and Activities
  • Neurobiology and Insect Physiology Research
  • Healthcare and Venom Research
  • Insect Resistance and Genetics
  • Biochemical and Structural Characterization
  • Insect and Arachnid Ecology and Behavior
  • Neuroscience and Neuropharmacology Research
  • Rabies epidemiology and control
  • Beetle Biology and Toxicology Studies
  • Entomological Studies and Ecology
  • Memory and Neural Mechanisms
  • Pain Mechanisms and Treatments
  • Toxin Mechanisms and Immunotoxins
  • Neurotransmitter Receptor Influence on Behavior
  • Receptor Mechanisms and Signaling
  • Marine Invertebrate Physiology and Ecology
  • Yersinia bacterium, plague, ectoparasites research
  • Amphibian and Reptile Biology
  • Spider Taxonomy and Behavior Studies
  • Chemical Synthesis and Analysis
  • Leech Biology and Applications

The University of Queensland
2015-2025

University of the Sunshine Coast
2020-2025

Ecologie des Forêts de Guyane
2020

Commonwealth Scientific and Industrial Research Organisation
2020

Agriculture and Food
2020

Centre National de la Recherche Scientifique
2020

Research Institute for Bioscience and Biotechnology
2019

Lewis & Clark College
2010

Monash University
2008

University of Tübingen
2002-2007

ArachnoServer ( www.arachnoserver.org ) is a manually curated database providing information on the sequence, structure and biological activity of protein toxins from spider venoms. These proteins are interest to wide range biologists due their diverse applications in medicine, neuroscience, pharmacology, drug discovery agriculture. currently manages 1078 sequences, 759 nucleic acid sequences 56 structures. Key features include molecular target ontology designed specifically for venom...

10.1093/nar/gkq1058 article EN cc-by-nc Nucleic Acids Research 2010-10-29

Abstract Human genetic studies have implicated the voltage-gated sodium channel Na V 1.7 as a therapeutic target for treatment of pain. A novel peptide, μ-theraphotoxin-Pn3a, isolated from venom tarantula Pamphobeteus nigricolor, potently inhibits (IC 50 0.9 nM) with at least 40–1000-fold selectivity over all other subtypes. Despite on-target activity in small-diameter dorsal root ganglia, spinal slices, and mouse model pain induced by activation, Pn3a alone displayed no analgesic formalin-,...

10.1038/srep40883 article EN cc-by Scientific Reports 2017-01-20

Significance Spider venom is a rich source of peptides, many targeting ion channels. We assessed peptide, Hm1a, as potential targeted therapy for Dravet syndrome, the genetic epilepsy linked to mutation in gene encoding sodium channel alpha subunit Na V 1.1. Cell-based assays showed Hm1a was selective hNa 1.1 over other and potassium Utilizing mouse model restored inhibitory neuron function significantly reduced seizures mortality heterozygote mice. Evidence from structure modeling suggest...

10.1073/pnas.1804764115 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2018-08-03

Abstract Summary ArachnoServer is a manually curated database that consolidates information on the sequence, structure, function and pharmacology of spider-venom toxins. Although spider venoms are complex chemical arsenals, primary constituents small disulfide-bridged peptides target neuronal ion channels receptors. Due to their high potency selectivity, these have been developed as pharmacological tools, bioinsecticides drug leads. A new version (v3.0) has includes bioinformatics pipeline...

10.1093/bioinformatics/btx661 article EN Bioinformatics 2017-10-18

The inhibitor cystine knot (ICK) is an unusual three-disulfide architecture in which one of the disulfide bonds bisects a loop formed by two other bridges and intervening sections protein backbone. Peptides containing ICK motif are frequently considered to have high levels thermal, chemical enzymatic stability due cross-bracing provided bonds. Experimental studies supporting this contention rare, particular for spider-venom toxins, represent largest diversity peptides. We used...

10.3390/toxins7104366 article EN cc-by Toxins 2015-10-26

Abstract The assassin bug venom system plays diverse roles in prey capture, defence and extra-oral digestion, but it is poorly characterised, partly due to its anatomical complexity. Here we demonstrate that this complexity results from numerous adaptations enable bugs modulate the composition of their a context-dependent manner. Gland reconstructions multimodal imaging reveal three distinct gland lumens: anterior main (AMG); posterior (PMG); accessory (AG). Transcriptomic proteomic...

10.1038/s41467-018-03091-5 article EN cc-by Nature Communications 2018-02-16

Spiders are one of the most successful venomous animals, with more than 48,000 described species. Most spider venoms dominated by cysteine-rich peptides a diverse range pharmacological activities. Some contain thousands unique peptides, but little is known about mechanisms used to generate such complex chemical arsenals. We an integrated transcriptomic, proteomic, and structural biology approach demonstrate that lethal Australian funnel-web produces 33 superfamilies venom proteins....

10.1073/pnas.1914536117 article EN Proceedings of the National Academy of Sciences 2020-05-12

Spider venoms are a rich source of ion channel modulators with therapeutic potential. Given the analgesic potential subtype-selective inhibitors voltage-gated sodium (NaV) channels, we screened spider for human NaV1.7 (hNaV1.7) using high-throughput fluorescent assay. Here, describe discovery novel inhibitor, μ-TRTX-Tp1a (Tp1a), isolated from venom Peruvian green-velvet tarantula Thrixopelma pruriens. Recombinant and synthetic forms this 33-residue peptide preferentially inhibited hNaV1.7 >...

10.1124/mol.115.098178 article EN Molecular Pharmacology 2015-05-15

Background and Purpose Chronic pain is a serious worldwide health issue, with current analgesics having limited efficacy dose‐limiting side effects. Humans loss‐of‐function mutations in the voltage‐gated sodium channel Na V 1.7 (h 1.7) are indifferent to pain, making h promising target for analgesic development. Since spider venoms replete modulators, we examined their potential as source of inhibitors. Experimental Approach We developed high‐throughput fluorescent‐based assay screen against...

10.1111/bph.13081 article EN British Journal of Pharmacology 2015-03-04

Although known for their potent venom and ability to prey upon both invertebrate vertebrate species, the Barychelidae spider family has been entirely neglected by toxinologists. In striking contrast, sister Theraphosidae (commonly as tarantulas), which last shared a most recent common ancestor with over 200 million years ago, received much attention, accounting 25% of all described toxins while representing only 2% species. this study, we evaluated first time arsenal barychelid spider,...

10.3390/toxins5122488 article EN cc-by Toxins 2013-12-13

Naturally occurring dysfunction of voltage-gated sodium (NaV ) channels results in complex disorders such as chronic pain, making these an attractive target for new therapies. In the pursuit novel NaV modulators, we investigated spider venoms inhibitors channels.We used high-throughput screens to identify a modulator venom Davus fasciatus. Further characterization this peptide was undertaken using fluorescent and electrophysiological assays, molecular modelling rodent pain model.We...

10.1111/bph.13865 article EN publisher-specific-oa British Journal of Pharmacology 2017-05-25
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