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Toxins
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Toxins-Membrane Interactions
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Toxins-Membrane Interactions

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

Deadline for manuscript submissions: closed (31 December 2018) | Viewed by 13301

Special Issue Editors

Dr. Christina I. Schroeder

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Guest Editor
Institute for Molecular Bioscience, The University of Queensland, Brisbane, 4072 QLD, Australia
Special Issues, Collections and Topics in MDPI journals
Assoc. Prof. Mehdi Mobli

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Guest Editor
Centre for Advanced Imaging, The University of Queensland, Brisbane, 4072 QLD, Australia

Special Issue Information

Dear Colleagues

Venom-derived toxins isolated from, e.g., spiders, snakes, scorpions, and cone snails, target a range of ion channels and receptors with high potency and sometime exquisite selectivity. These toxins have played an important part in furthering our understanding of the pharmacology and physiology of these ion channels and receptors, many of which are involved in various pathophysiological conditions, including pain, stroke, cardiac disease and epilepsy and they are therefore also being pursued as interesting drug leads. Interestingly, in addition to targeting membrane proteins, several toxins have been reported to target the membrane itself and in some instances, interact with both the membrane and the membrane protein in a tri-molecular complex. In this Special Issue, we are therefore focusing on toxin-membrane interactions. We are welcoming submission with an emphasis on membrane-interacting toxins, membrane-permeating toxins and toxins that interact with the membrane and a membrane protein in concert with the aim of shining the spotlight on an understudied area in the field of toxin drug development. The study of toxin-membrane interactions could potentially challenge the traditional lock-and key paradigm employed in drug design. It is therefore crucial that we further our knowledge of toxin-membrane interactions if we are to understand, e.g., cell-penetrating toxins or toxin-receptor subtype selectivity.

Dr. Christina I. Schroeder
Assoc. Prof. Mehdi Mobli
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 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 2700 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

  • toxins
  • lipid membranes
  • toxin-membrane interactions
  • membrane-permeating toxins
  • trimolecular complex
  • toxin-membrane molecular modelling
  • toxin biophysical studies
  • toxin engineering

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Published Papers (3 papers)

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Research

15 pages, 1694 KiB  
Article
New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado
by Katsuhiro Konno, Kohei Kazuma, Marisa Rangel, Joacir Stolarz-de-Oliveira, Renato Fontana, Marii Kawano, Hiroyuki Fuchino, Izumi Hide, Tadashi Yasuhara and Yoshihiro Nakata
Toxins 2019, 11(3), 155; https://doi.org/10.3390/toxins11030155 - 10 Mar 2019
Cited by 19 | Viewed by 4155
Abstract
Comprehensive LC-MS and MS/MS analysis of the crude venom extract from the solitary eumenine wasp Eumenes micado revealed the component profile of this venom mostly consisted of small peptides. The major peptide components, eumenine mastoparan-EM1 (EMP-EM1: LKLMGIVKKVLGAL-NH2) and eumenine mastoparan-EM2 (EMP-EM2: [...] Read more.
Comprehensive LC-MS and MS/MS analysis of the crude venom extract from the solitary eumenine wasp Eumenes micado revealed the component profile of this venom mostly consisted of small peptides. The major peptide components, eumenine mastoparan-EM1 (EMP-EM1: LKLMGIVKKVLGAL-NH2) and eumenine mastoparan-EM2 (EMP-EM2: LKLLGIVKKVLGAI-NH2), were purified and characterized by the conventional method. The sequences of these new peptides are homologous to mastoparans, the mast cell degranulating peptides from social wasp venoms; they are 14 amino acid residues in length, rich in hydrophobic and basic amino acids, and C-terminal amidated. Accordingly, these new peptides can belong to mastoparan peptides (in other words, linear cationic α-helical peptides). Indeed, the CD spectra of these new peptides showed predominantly α-helix conformation in TFE and SDS. In biological evaluation, both peptides exhibited potent antibacterial activity, moderate degranulation activity from rat peritoneal mast cells, and significant leishmanicidal activity, while they showed virtually no hemolytic activity on human or mouse erythrocytes. These results indicated that EMP-EM peptides rather strongly associated with bacterial cell membranes rather than mammalian cell membranes. Full article
(This article belongs to the Special Issue Toxins-Membrane Interactions)
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29 pages, 20729 KiB  
Article
Naja mossambica mossambica Cobra Cardiotoxin Targets Mitochondria to Disrupt Mitochondrial Membrane Structure and Function
by Boris Zhang, Feng Li, Zhengyao Chen, Indira H. Shrivastava, Edward S. Gasanoff and Ruben K. Dagda
Toxins 2019, 11(3), 152; https://doi.org/10.3390/toxins11030152 - 8 Mar 2019
Cited by 32 | Viewed by 4814
Abstract
Cobra venom cardiotoxins (CVCs) can translocate to mitochondria to promote apoptosis by eliciting mitochondrial dysfunction. However, the molecular mechanism(s) by which CVCs are selectively targeted to the mitochondrion to disrupt mitochondrial function remains to be elucidated. By studying cardiotoxin from Naja mossambica mossambica [...] Read more.
Cobra venom cardiotoxins (CVCs) can translocate to mitochondria to promote apoptosis by eliciting mitochondrial dysfunction. However, the molecular mechanism(s) by which CVCs are selectively targeted to the mitochondrion to disrupt mitochondrial function remains to be elucidated. By studying cardiotoxin from Naja mossambica mossambica cobra (cardiotoxin VII4), a basic three-fingered S-type cardiotoxin, we hypothesized that cardiotoxin VII4 binds to cardiolipin (CL) in mitochondria to alter mitochondrial structure/function and promote neurotoxicity. By performing confocal analysis, we observed that red-fluorescently tagged cardiotoxin rapidly translocates to mitochondria in mouse primary cortical neurons and in human SH-SY5Y neuroblastoma cells to promote aberrant mitochondrial fragmentation, a decline in oxidative phosphorylation, and decreased energy production. In addition, by employing electron paramagnetic resonance (EPR) and protein nuclear magnetic resonance (1H-NMR) spectroscopy and phosphorescence quenching of erythrosine in model membranes, our compiled biophysical data show that cardiotoxin VII4 binds to anionic CL, but not to zwitterionic phosphatidylcholine (PC), to increase the permeability and formation of non-bilayer structures in CL-enriched membranes that biochemically mimic the outer and inner mitochondrial membranes. Finally, molecular dynamics simulations and in silico docking studies identified CL binding sites in cardiotoxin VII4 and revealed a molecular mechanism by which cardiotoxin VII4 interacts with CL and PC to bind and penetrate mitochondrial membranes. Full article
(This article belongs to the Special Issue Toxins-Membrane Interactions)
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15 pages, 5286 KiB  
Article
Purification and Characterization of JZTx-14, a Potent Antagonist of Mammalian and Prokaryotic Voltage-Gated Sodium Channels
by Jie Zhang, Dongfang Tang, Shuangyu Liu, Haoliang Hu, Songping Liang, Cheng Tang and Zhonghua Liu
Toxins 2018, 10(10), 408; https://doi.org/10.3390/toxins10100408 - 10 Oct 2018
Cited by 4 | Viewed by 3635
Abstract
Exploring the interaction of ligands with voltage-gated sodium channels (NaVs) has advanced our understanding of their pharmacology. Herein, we report the purification and characterization of a novel non-selective mammalian and bacterial NaVs toxin, JZTx-14, from the venom of the [...] Read more.
Exploring the interaction of ligands with voltage-gated sodium channels (NaVs) has advanced our understanding of their pharmacology. Herein, we report the purification and characterization of a novel non-selective mammalian and bacterial NaVs toxin, JZTx-14, from the venom of the spider Chilobrachys jingzhao. This toxin potently inhibited the peak currents of mammalian NaV1.2–1.8 channels and the bacterial NaChBac channel with low IC50 values (<1 µM), and it mainly inhibited the fast inactivation of the NaV1.9 channel. Analysis of NaV1.5/NaV1.9 chimeric channel showed that the NaV1.5 domain II S3–4 loop is involved in toxin association. Kinetics data obtained from studying toxin–NaV1.2 channel interaction showed that JZTx-14 was a gating modifier that possibly trapped the channel in resting state; however, it differed from site 4 toxin HNTx-III by irreversibly blocking NaV currents and showing state-independent binding with the channel. JZTx-14 might stably bind to a conserved toxin pocket deep within the NaV1.2–1.8 domain II voltage sensor regardless of channel conformation change, and its effect on NaVs requires the toxin to trap the S3–4 loop in its resting state. For the NaChBac channel, JZTx-14 positively shifted its conductance-voltage (G–V) and steady-state inactivation relationships. An alanine scan analysis of the NaChBac S3–4 loop revealed that the 108th phenylalanine (F108) was the key residue determining the JZTx-14–NaChBac interaction. In summary, this study provided JZTx-14 with potent but promiscuous inhibitory activity on both the ancestor bacterial NaVs and the highly evolved descendant mammalian NaVs, and it is a useful probe to understand the pharmacology of NaVs. Full article
(This article belongs to the Special Issue Toxins-Membrane Interactions)
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