Reprint
Arthropod Venom Components and Their Potential Usage
Edited by
March 2020
404 pages
- ISBN978-3-03928-540-2 (Paperback)
- ISBN978-3-03928-541-9 (PDF)
This book is a reprint of the Special Issue Arthropod Venom Components and Their Potential Usage that was published in
Biology & Life Sciences
Medicine & Pharmacology
Public Health & Healthcare
Summary
Thousands of arthropod species, ranging from arachnids (spiders and scorpions) to hymenopterans (ants, bees, and wasps) and myriapods (centipedes), are venomous and use their venoms for both defense and predation. These venoms are invariably harmful to humans, and some may cause serious injuries, e.g., those from scorpions, spiders, and wasps. Arthropods’ venoms are also known as rich sources of biologically active compounds and have attracted the attention of toxin researchers for years. In this century, venom component analysis has progressed considerable due to the advances in analytical techniques, in particular, mass spectrometry and next-generation deep (DNA and RNA) sequencing. As such, proteomic and peptidomic analyses using LC–MS have enabled the full analysis of venom components, revealing a variety of novel peptide and protein toxins sequences and scaffolds, potentially useful as pharmacological research tools and for the development of highly selective peptide ligands and therapeutic leads, like chlorotoxin. Due to their specificity for numerous ion-channel subtypes, including voltage- and ligand-gated ion channels, arthropod neurotoxins have been investigated to dissect and treat neurodegenerative diseases and control epileptic syndromes. This Special Issue collects information on such progress, encouraging contributions on the chemical and biological characterization of venom components, not only peptides and proteins, but also small molecules, their mechanisms of action, and the development of venom-derived peptide leads.
Format
- Paperback
License
© 2020 by the authors; CC BY-NC-ND license
Keywords
ant; venom; mass spectrometry analysis; pilosulin-like peptide; phospholipases D; metalloproteases; Loxosceles spp.; recombinant toxins; hybrid immunogen; neutralizing antibodies; antivenoms; LyeTxI-b; Staphylococcus aureus; keratitis; AMP; mastoparan; Acinetobacter baumannii; stent; cantharidin; blister beetle; Berberomeloe majalis; nematicide; ixodicide; antifeedant; scorpion venom; insecticidal peptide; mass spectrometric analysis; de novo sequencing; Centruroides limpidus Karch; proteome; scorpion; transcriptome; venom toxicity; brown spider; venom; Loxosceles; toxins; biotools; drug targets; novel therapeutics; spider toxin; directed disulfide bond formation; Nav channel activity; Nav1.7; pain target; automated patch-clamp; bee venom; alternative treatment; skin; cutaneous disease; mechanism; chemotherapy; cold allodynia; mechanical allodynia; melittin; neuropathic pain; oxaliplatin; natural antibiotics; piperidine heterocyclic amines; industrial biotechnology; LTQ Orbitrap Hybrid Mass Spectrometer; myrmecology; venom; pain; ants; wasps; bees; Hymenoptera; envenomation; toxins; peptides; pharmacology; Dinoponera quadriceps; Formicidae; Hymenoptera venom; proteomics; venom allergens; ICK-like toxins; melittin; insect immune system; apoptosis; heart contractility; Tenebrio molitor; bee venom; bioinformatics; computational docking; homology modelling; ion channel structure; protein–peptide interactions; tertiapin; venom peptides; virtual screening; small hive beetle; solitary wasp; venom; antimicrobial peptide; linear cationic α-helical peptide; amphipathic α-helix structure; channel-like pore-forming activity; antimicrobial peptide; venom; arthropod; malaria; Chagas disease; human African trypanosomiasis; leishmaniasis; toxoplasmosis; venom peptides; FMRF-amide; insect neurotoxin; protons; pH regulation; acid-sensing ion channels; acid-gated currents; chronic pain; ICK peptide; knottins; NaV; spider venom; voltage-gated sodium channel; n/a