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Special Issue "Arthropod Venom Components and their Potential Usage"

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: 31 May 2019

Special Issue Editors

Guest Editor
Dr. Katsuhiro Konno

Institute of Natural Medicine, University of Toyama, Toyama 930-0194, Japan
Website | E-Mail
Interests: Chemistry (isolation, structure, and synthesis) of natural products; solitary wasp and ant venom peptides; sea anemone toxins, spider toxins
Guest Editor
Prof. Dr. Gandhi Rádis-Baptista

Laboratory of Biochemistry and Biotechnology, Institute for Marine Sciences, Federal University of Ceara, Fortaleza, 60165-081 CE, Brazil
Website 1 | Website 2 | E-Mail
Interests: Transcriptome of arthropods, cnidarians and other venomous animals; peptide engineering; anti-proliferative peptides; membranolytic peptides; pharmaceutical biotechnology

Special Issue Information

Dear Colleagues,

Thousands of arthropod species, ranging from arachnids (spiders and scorpions) to hymenopterans (ants, bees, and wasps) and myriapods (centipedes), are venomous and utilize their venoms for both defending themselves and predating preys. These venoms are invariably harmful to humans, and some may cause serious injuries, e.g., those from scorpions, spiders, and wasps. On the other hand, arthropods’ venoms have been known as rich sources of biologically active compounds and have attracted the attention of toxin researchers for years. Especially in this century, venom component analysis has progressed much more than ever because of the great advances of analytical techniques, in particular, mass spectrometry and next-generation deep (DNA and RNA) sequencing. As such, proteomic and peptidomic analyses utilizing LC–MS, as well as transcriptomics - alone or in combination with proteomics, have made it possible to fully analyze venoms’ 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. Because of 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 will collect 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.

Prof. Dr. Katsuhiro Konno
Prof. Dr. Gandhi Rádis-Baptista
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • venom components
  • peptide toxins
  • protein toxins
  • proteomics
  • peptidomics
  • transcriptome
  • venomics
  • peptide ligand
  • peptide engineering
  • venom-derived peptide leads

Published Papers (2 papers)

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Research

Open AccessArticle Design and Production of a Recombinant Hybrid Toxin to Raise Protective Antibodies against Loxosceles Spider Venom
Received: 16 January 2019 / Revised: 8 February 2019 / Accepted: 10 February 2019 / Published: 12 February 2019
PDF Full-text (2613 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Human accidents with spiders of the genus Loxosceles are an important health problem affecting thousands of people worldwide. Patients evolve to severe local injuries and, in many cases, to systemic disturbances as acute renal failure, in which cases antivenoms are considered to be [...] Read more.
Human accidents with spiders of the genus Loxosceles are an important health problem affecting thousands of people worldwide. Patients evolve to severe local injuries and, in many cases, to systemic disturbances as acute renal failure, in which cases antivenoms are considered to be the most effective treatment. However, for antivenom production, the extraction of the venom used in the immunization process is laborious and the yield is very low. Thus, many groups have been exploring the use of recombinant Loxosceles toxins, particularly phospholipases D (PLDs), to produce the antivenom. Nonetheless, some important venom activities are not neutralized by anti-PLD antibodies. Astacin-like metalloproteases (ALMPs) are the second most expressed toxin acting on the extracellular matrix, indicating the importance of its inclusion in the antigen’s formulation to provide a better antivenom. Here we show the construction of a hybrid recombinant immunogen, called LgRec1ALP1, composed of hydrophilic regions of the PLD and the ALMP toxins from Loxosceles gaucho. Although the LgRec1ALP1 was expressed as inclusion bodies, it resulted in good yields and it was effective to produce neutralizing antibodies in mice. The antiserum neutralized fibrinogenolytic, platelet aggregation and dermonecrotic activities elicited by L. gaucho, L. laeta, and L. intermedia venoms, indicating that the hybrid recombinant antigen may be a valuable source for the production of protective antibodies against Loxosceles ssp. venoms. In addition, the hybrid recombinant toxin approach may enrich and expand the alternative antigens for antisera production for other venoms. Full article
(This article belongs to the Special Issue Arthropod Venom Components and their Potential Usage)
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Open AccessArticle Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components
Received: 5 December 2018 / Revised: 9 January 2019 / Accepted: 12 January 2019 / Published: 17 January 2019
PDF Full-text (2534 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
We previously identified 92 toxin-like peptides and proteins, including pilosulin-like peptides 1–6 from the predatory ant Odontomachus monticola, by transcriptome analysis. Here, to further characterize venom components, we analyzed the venom and venom sac extract by ESI-MS/MS with or without trypsin digestion [...] Read more.
We previously identified 92 toxin-like peptides and proteins, including pilosulin-like peptides 1–6 from the predatory ant Odontomachus monticola, by transcriptome analysis. Here, to further characterize venom components, we analyzed the venom and venom sac extract by ESI-MS/MS with or without trypsin digestion and reducing agent. As the low-molecular-mass components, we found amino acids (leucine/isoleucine, phenylalanine, and tryptophan) and biogenic amines (histamine and tyramine) in the venom and venom sac extract. As the higher molecular mass components, we found peptides and proteins such as pilosulin-like peptides, phospholipase A2s, hyaluronidase, venom dipeptidyl peptidases, conotoxin-like peptide, and icarapin-like peptide. In addition to pilosulin-like peptides 1–6, we found three novel pilosulin-like peptides that were overlooked by transcriptome analysis. Moreover, pilosulin-like peptides 1–6 were chemically synthesized, and some of them displayed antimicrobial, hemolytic, and histamine-releasing activities. Full article
(This article belongs to the Special Issue Arthropod Venom Components and their Potential Usage)
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