Peptide toxins from the longest animal on earth

Planta Medica ◽  
2016 ◽  
Vol 81 (S 01) ◽  
pp. S1-S381
Author(s):  
E Jacobsson ◽  
HS Andersson ◽  
M Strand ◽  
E Lebbe ◽  
C Eriksson ◽  
...  
Keyword(s):  
Peptide Toxins

scholarly journals Snails In Silico: A Review of Computational Studies on the Conopeptides

Marine Drugs ◽  
2019 ◽  
Vol 17 (3) ◽  
pp. 145 ◽  
Author(s):  
Rachael Mansbach ◽  
Timothy Travers ◽  
Benjamin McMahon ◽  
Jeanne Fair ◽  
S. Gnanakaran
Keyword(s):  
Posttranslational Modifications ◽  
High Throughput Screening ◽  
Molecular Mechanisms ◽  
Defense Mechanism ◽  
Docking Studies ◽  
Chemical Diversity ◽  
Machine Learning Techniques ◽  
Peptide Toxins ◽  
Dynamics Simulations ◽  
And Function

Marine cone snails are carnivorous gastropods that use peptide toxins called conopeptides both as a defense mechanism and as a means to immobilize and kill their prey. These peptide toxins exhibit a large chemical diversity that enables exquisite specificity and potency for target receptor proteins. This diversity arises in terms of variations both in amino acid sequence and length, and in posttranslational modifications, particularly the formation of multiple disulfide linkages. Most of the functionally characterized conopeptides target ion channels of animal nervous systems, which has led to research on their therapeutic applications. Many facets of the underlying molecular mechanisms responsible for the specificity and virulence of conopeptides, however, remain poorly understood. In this review, we will explore the chemical diversity of conopeptides from a computational perspective. First, we discuss current approaches used for classifying conopeptides. Next, we review different computational strategies that have been applied to understanding and predicting their structure and function, from machine learning techniques for predictive classification to docking studies and molecular dynamics simulations for molecular-level understanding. We then review recent novel computational approaches for rapid high-throughput screening and chemical design of conopeptides for particular applications. We close with an assessment of the state of the field, emphasizing important questions for future lines of inquiry.

Cellular effects of cyanobacterial peptide toxins

1988 ◽  
Vol 3 (5) ◽  
pp. 511-518 ◽  
Author(s):  
J. E. Eriksson ◽  
J. A. O. Meriluoto ◽  
H. P. Kujari ◽  
K. Jamel Al-Layl ◽  
G. A. Codd
Keyword(s):  
Cellular Effects ◽  
Peptide Toxins

scholarly journals Ribosomal biosynthesis of the cyclic peptide toxins of Amanita mushrooms

Biopolymers ◽  
2010 ◽  
Vol 94 (5) ◽  
pp. 659-664 ◽  
Author(s):  
Jonathan D. Walton ◽  
Heather E. Hallen-Adams ◽  
Hong Luo
Keyword(s):  
Cyclic Peptide ◽  
Peptide Toxins ◽  
Amanita Mushrooms

scholarly journals Molecular identification of poisonous mushrooms using nuclear ITS region and peptide toxins: a retrospective study on fatal cases in Thailand

2016 ◽  
Vol 41 (1) ◽  
pp. 65-76 ◽  
Author(s):  
Sittiporn Parnmen ◽  
Sujitra Sikaphan ◽  
Siriwan Leudang ◽  
Thitiya Boonpratuang ◽  
Achariya Rangsiruji ◽  
...  
Keyword(s):  
Retrospective Study ◽  
Molecular Identification ◽  
Its Region ◽  
Nuclear Its ◽  
Peptide Toxins ◽  
Poisonous Mushrooms

scholarly journals Novel Cyclic Peptides from Lethal Amanita Mushrooms through a Genome-Guided Approach

2021 ◽  
Vol 7 (3) ◽  
pp. 204
Author(s):  
Shengwen Zhou ◽  
Xincan Li ◽  
Yunjiao Lüli ◽  
Xuan Li ◽  
Zuo H. Chen ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cyclic Peptides ◽  
Cyclic Peptide ◽  
Amino Acid Residues ◽  
Fragment Ions ◽  
Peptide Pair ◽  
A Genome ◽  
Peptide Toxins ◽  
Poisonous Mushrooms ◽  
Large Peptide

Most species in the genus Amanita are ectomycorrhizal fungi comprising both edible and poisonous mushrooms. Some species produce potent cyclic peptide toxins, such as α-amanitin, which places them among the deadliest organisms known to mankind. These toxins and related cyclic peptides are encoded by genes of the “MSDIN” family (named after the first five amino acid residues of the precursor peptides), and it is largely unknown to what extent these genes are expressed in the basidiocarps. In the present study, Amanita rimosa and Amanita exitialis were sequenced through the PacBio and Illumina techniques. Together with our two previously sequenced genomes, Amanita subjunquillea and Amanita pallidorosea, in total, 46 previously unknown MSDIN genes were discovered. The expression of over 80% of the MSDIN genes was demonstrated in A. subjunquillea. Through a combination of genomics and mass spectrometry, 12 MSDIN genes were shown to produce novel cyclic peptides. To further confirm the results, three of the cyclic peptides were chemically synthesized. The tandem mass spectrometry (MS/MS) spectra of the natural and the synthetic peptides shared a majority of the fragment ions, demonstrating an identical structure between each peptide pair. Collectively, the results suggested that the genome-guided approach is reliable for identifying novel cyclic peptides in Amanita species and that there is a large peptide reservoir in these mushrooms.

scholarly journals Variation of Two S3b Residues in KV4.1–4.3 Channels Underlies Their Different Modulations by Spider Toxin κ-LhTx-1

2021 ◽  
Vol 12 ◽  
Author(s):  
Zhen Xiao ◽  
Piao Zhao ◽  
Xiangyue Wu ◽  
Xiangjin Kong ◽  
Ruiwen Wang ◽  
...  
Keyword(s):  
Mutation Analysis ◽  
Voltage Dependence ◽  
Underlying Mechanism ◽  
Voltage Sensor ◽  
Action Mode ◽  
Gating Modifier ◽  
Peptide Toxin ◽  
Peptide Toxins ◽  
Key Residues ◽  
Animal Venoms

The naturally occurred peptide toxins from animal venoms are valuable pharmacological tools in exploring the structure-function relationships of ion channels. Herein we have identified the peptide toxin κ-LhTx-1 from the venom of spider Pandercetes sp (the Lichen huntsman spider) as a novel selective antagonist of the KV4 family potassium channels. κ-LhTx-1 is a gating-modifier toxin impeded KV4 channels’ voltage sensor activation, and mutation analysis has confirmed its binding site on channels’ S3b region. Interestingly, κ-LhTx-1 differently modulated the gating of KV4 channels, as revealed by toxin inhibiting KV4.2/4.3 with much more stronger voltage-dependence than that for KV4.1. We proposed that κ-LhTx-1 trapped the voltage sensor of KV4.1 in a much more stable resting state than that for KV4.2/4.3 and further explored the underlying mechanism. Swapping the non-conserved S3b segments between KV4.1(280FVPK283) and KV4.3(275VMTN278) fully reversed their voltage-dependence phenotypes in inhibition by κ-LhTx-1, and intensive mutation analysis has identified P282 in KV4.1, D281 in KV4.2 and N278 in KV4.3 being the key residues. Furthermore, the last two residues in this segment of each KV4 channel (P282/K283 in KV4.1, T280/D281 in KV4.2 and T277/N278 in KV4.3) likely worked synergistically as revealed by our combinatorial mutations analysis. The present study has clarified the molecular basis in KV4 channels for their different modulations by κ-LhTx-1, which have advanced our understanding on KV4 channels’ structure features. Moreover, κ-LhTx-1 might be useful in developing anti-arrhythmic drugs given its high affinity, high selectivity and unique action mode in interacting with the KV4.2/4.3 channels.

scholarly journals TOXIC AND IMMUNE ALLERGIC RESPONSES OF ANT VENOM TOXINS: A REVIEW

2021 ◽  
pp. 1-7
Author(s):  
SIMRAN SHARMA ◽  
RAVI KANT UPADHYAY!
Keyword(s):  
Immune Responses ◽  
Biological Effects ◽  
Therapeutic Agents ◽  
Microbial Pathogens ◽  
Intense Pain ◽  
Venom Toxins ◽  
Potential Source ◽  
Ant Venom ◽  
Peptide Toxins ◽  
Promising Source

Present review article explains ant venom components and its allergic and biological effects in man and animals. Red ants or small fire ants secrete and inject venom very swiftly to defend their nest against predators, microbial pathogens, and competitors and to hunt the prey. Ant venom is a mixture of various organic compounds, including peptides, enzymes, and polypeptide toxins. It is highly toxic, allergic, invasive and venomous. It imposes sever paralytic, cytolytic, haemolytic, allergenic, pro-inflammatory, insecticidal, antimicrobial, and pain-producing pharmacologic activities after infliction. Victims show red ring-shaped allergic sign with regional swelling marked with intense pain. Ant venom also contains several hydrolases, oxidoreductases, proteases, Kunitz-like polypeptides, and inhibitor cysteine knot (ICK)-like (knottin) neurotoxins and insect defensins. Ant venom toxins/proteins generate allergic immune responses and employ eosinophils and produce Th2 cytokines, response. These compounds from ant venom could be used as a potential source of new anticonvulsants molecules. Ant venoms contain many small, linear peptides, an untapped source of bioactive peptide toxins. The remarkable insecticidal activity of ant venom could be used as a promising source of additional bio-insecticides and therapeutic agents.

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