Reprint

Identification and Functional Characterization of Novel Venom Components

Edited by
August 2020
210 pages
  • ISBN978-3-03936-467-1 (Hardback)
  • ISBN978-3-03936-468-8 (PDF)

This book is a reprint of the Special Issue Identification and Functional Characterization of Novel Venom Components that was published in

Biology & Life Sciences
Medicine & Pharmacology
Public Health & Healthcare
Summary

Throughout most of the 20th century, the toxinological literature consisted largely of pharmacological and functional characterizations of crude venoms and venom constituents, often constituents that could not be identified unambiguously. The advent of amino acid composition analysis in the 1950s enabled the first forays into physical characterizations of purified toxins, though these remained few in number until the 1970s. Then, the tryptic and chymotryptic cleavage of venom proteins coupled with manual Edman degradation began to provide the first complete sequences, particularly of three-finger toxins. Polyacrylamide gel electrophoresis and improved resins for liquid chromatography permitted improved purification and better gross structural characterization of venom components. The early 1980s witnessed the advent of automated Edman degradation, and entire sequences of longer proteins began to be reported in the literature. Then, the molecular biology revolution enabled the generation of cDNA sequences of more and larger proteins, followed by mass-spectrometry-based proteomics and quantitative high-throughput DNA sequencing and genomics.  Today, we face an unprecedented situation in which our capacity to generate sequence/structural data has completely overwhelmed our capacity to functionally characterize venom constituents. This Special Issue of Toxins includes 11 publications addressing the discovery and functional characterization of novel venom constituents of vertebrate and invertebrate venoms.

Format
  • Hardback
License
© 2020 by the authors; CC BY-NC-ND license
Keywords
bradykinin-related peptide (BRP); RVA-Thr6-BK; site-substitution variant; agonist; antagonist; myotropic actions; amidation; evolution; posttranslational modifications; scorpion; transcriptomics; natriuretic peptide; myocardial infarction; ischemia-reperfusion injury; inflammation; fibrosis; mass spectrometry; LC-MS; Formicidae; Myrmicinae; Myrmica rubra; venom gland; bioinsecticide; antimicrobial peptide; aphids; Acyrthosiphon pisum; snake venom; phosphodiesterases; amino acid sequence and three-dimensional structural analysis; variable substrate specificity; PDE_Ca structure–function relationship; evolutionary shifts; Hadruridae; negative selection; phylogenomics; venom transcriptome; snake venom; Agkistrodon contortrix pictigaster; D49 PLA2; homologous K49 PLA2; myotoxin; edema-forming activity and cytotoxicity; arterial thrombosis; antiplatelet agent; integrin αIIbβ3; bleeding side effect; snake venom proteins; disintegrins; CAP superfamily; ion channel blockage; salivary component; co-factors; small serum proteins; Protobothrops flavoviridis; evolution; gene array; comparative genomics; snake venoms; antimicrobial peptides; anticancer peptides; cathelicidin; defensin; crotamine; snake venom proteins; snake venom peptides; n/a