Pathogens and Natural Toxins

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

Deadline for manuscript submissions: closed (25 February 2023) | Viewed by 2864

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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

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Keywords

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

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Published Papers (1 paper)

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Research

15 pages, 5709 KiB  
Article
Pore-Forming Cardiotoxin VVA2 (Volvatoxin A2) Variant I82E/L86K Is an Atypical Duplex-Specific Nuclease
by Jia-Qi Lu, Jia-Wen Shou, Ka-Ching Lo, Yun-Sang Tang, Wei-Wei Shi and Pang-Chui Shaw
Toxins 2022, 14(6), 392; https://doi.org/10.3390/toxins14060392 - 6 Jun 2022
Viewed by 2051
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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