Special Issue "Pathogens and Natural Toxins"

A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: 25 February 2023 | Viewed by 862

Special Issue Editor

Dr. Bryan Grieg Fry
E-Mail Website
Guest Editor
Venom Evolution Laboratory, School of Biological Sciences, University of Queensland, St. Lucia, QLD 4072, Australia
Interests: venom molecular evolution; phylogenetics and structure–function relationships; toxins
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The Pathogens and Natural Toxins e-conference (https://sciforum.net/event/PNTEC) brings together a wide range of disciplines, from toxinology to ecology to animal behaviour. This will allow for a more holistic investigation of microbial and animal toxins as well as pathogenic organisms. This Special Issue is open to any paper that fits within this very broad theme and from any author, not just those who are involved in the e-conference. Of particular interest will be those papers which address broad conceptual issues that span multiple taxon or toxin classes, or are multidisciplinary, such as investigating how evolutionary selection pressures on independently toxic or pathogenic lineages have resulted in convergent clinical effects. It is hoped that this novel approach will bring together scientists from fields which do not normally intersect, in order to facilitate a broad and dynamic investigation of the toxic and pathogenic world around us.

Dr. Bryan Grieg Fry
Guest Editor

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 submissions that pass pre-check are 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 2400 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

  • toxin
  • venom
  • virus
  • bacteria
  • plant
  • fungi
  • pathogen
  • antitoxin
  • antivenom
  • drug design

Published Papers (1 paper)

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Research

Article
Pore-Forming Cardiotoxin VVA2 (Volvatoxin A2) Variant I82E/L86K Is an Atypical Duplex-Specific Nuclease
Toxins 2022, 14(6), 392; https://doi.org/10.3390/toxins14060392 - 06 Jun 2022
Viewed by 588
Abstract
VVA2 (volvatoxin A chain 2) is a cardiotoxic protein purified from Volvariella volvacea. Its biological activities include hemolysis, writhing reaction, neurotoxicity, and ventricular systolic arresting activity. The cytotoxicity of VVA2 was mainly considered due to its pore-forming activity. Here we report a [...] Read more.
VVA2 (volvatoxin A chain 2) is a cardiotoxic protein purified from Volvariella volvacea. Its biological activities include hemolysis, writhing reaction, neurotoxicity, and ventricular systolic arresting activity. The cytotoxicity of VVA2 was mainly considered due to its pore-forming activity. Here we report a novel biological activity of its variants VVA2 I82E/K86K as a duplex-specific nuclease. Recombinant VVA2 variant I82E/L86K (Re-VVA2 I82E/L86K), deprived of the oligomerization property, shows increased nuclease activity compared to VVA2. Re-VVA2 I82E/L86K converts supercoiled DNA (Replicative form I, RF I) into nicked form (RF II) and linear form (RF III) in the presence of Mg2+ or Mn2+. Besides plasmid DNA, it also exhibits nuclease activity on E. coli genomic DNA rather than ssDNA or RNA. Re-VVA2 I82E/L86K preferentially cleaves dG-dC-rich dsDNA regions and shows the best performance at pH 6–9 and 55 °C. Our structure–function study has revealed amino acid E111 may take an active part in nuclease activity through interacting with metal ions. Based on the sequences of its cleavage sites, a “double-hit” mechanism was thereby proposed. Given that Re-VVA2 I82E/L86K did not exhibit the conserved nuclease structure and sequence, it is considered an atypical duplex-specific nuclease. Full article
(This article belongs to the Special Issue Pathogens and Natural Toxins)
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