Molecular diversity and evolutionary trends of cysteine-rich peptides from the venom glands of Chinese spider Heteropoda venatoria

2020 ◽  
Author(s):  
Yiying Ding ◽  
Kezhi Chen ◽  
Xuewen Zhang ◽  
Tiaoyi Xiao ◽  
Jinjun Chen
Keyword(s):  
Insect Pests ◽  
Venom Gland ◽  
Evolutionary Analysis ◽  
Evolutionary Trends ◽  
Holistic View ◽  
Carl Linnaeus ◽  
Peptide Precursor ◽  
Venom Glands ◽  
Peptide Toxin ◽  
Peptide Toxins

Abstract Background: The huntsman spider ( Heteropoda venatoria Carl Linnaeus, 1767) in family Sparassidae, is highly valued in tropical and subtropical countries because the species capture and feed on cockroaches and other domestic insect pests. Unlike most other species of Araneomorphae, the huntsman spiders do not use webs to capture prey. Their great speed and strong chelicerae (mouthparts) with toxin glands are used to capture the insects.Results: We identified 154 novel putative cysteine-rich peptide toxin precursors by analyzing expressed sequence tags of the spider H. venatoria venom gland. The sequences of cysteine-rich peptide precursor revealed 24 families based on the phylogenetics analyses of signal peptide and cysteine framework in mature region, including 8 families of classic Inhibitory cystine knot toxins, 2 families of novel 6-cys motifs, 13 families of long cysteine-rich peptides with 8, 10 and 12-cys, and one family of 2-cys peptides. Intriguingly, four kinds of motifs are first described in spider venom. Furthermore, combining the diverse cysteine-rich peptide sequences of H. venatoria with the sequences from represent spiders explored previously, the dynamic evolutionary trends of venom cysteine-rich peptides were investigated based on the analysis of the structures of precursors and the patterns of cysteine scaffolds in the phylogenetic framework.Conclusion: H. venatoria is an appropriate intermediate species for the evolutionary analysis of spider peptide toxins from Mygalomorphae to Araneomorphae with a holistic view. This work revealed the dynamic evolutionary trends of venom cysteine-rich peptides of spider: the mature peptides have been developed longer with more cysteines; and the propeptides between the signal and mature peptides have been diminished and even vanished. With respect to potential insecticidal applications, the work provides promising new templates and gene clones for further exploration.

scholarly journals Molecular diversity and evolutionary trends of cysteine-rich peptides from the venom glands of Chinese spider Heteropoda venatoria

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jie Luo ◽  
Yiying Ding ◽  
Zhihao Peng ◽  
Kezhi Chen ◽  
Xuewen Zhang ◽  
...  
Keyword(s):  
Expressed Sequence Tags ◽  
Molecular Diversity ◽  
Insect Pests ◽  
Phylogenetic Analyses ◽  
Spider Venom ◽  
Evolutionary Trends ◽  
The Family ◽  
Venom Glands ◽  
Venom Evolution ◽  
Expressed Sequence

AbstractHeteropoda venatoria in the family Sparassidae is highly valued in pantropical countries because the species feed on domestic insect pests. Unlike most other species of Araneomorphae, H. venatoria uses the great speed and strong chelicerae (mouthparts) with toxin glands to capture the insects instead of its web. Therefore, H. venatoria provides unique opportunities for venom evolution research. The venom of H. venatoria was explored by matrix-assisted laser desorption/ionization tandem time-of-flight and analyzing expressed sequence tags. The 154 sequences coding cysteine-rich peptides (CRPs) revealed 24 families based on the phylogenetic analyses of precursors and cysteine frameworks in the putative mature regions. Intriguingly, four kinds of motifs are first described in spider venom. Furthermore, combining the diverse CRPs of H. venatoria with previous spider venom peptidomics data, the structures of precursors and the patterns of cysteine frameworks were analyzed. This work revealed the dynamic evolutionary trends of venom CRPs in H. venatoria: the precursor has evolved an extended mature peptide with more cysteines, and a diminished or even vanished propeptides between the signal and mature peptides; and the CRPs evolved by multiple duplications of an ancestral ICK gene as well as recruitments of non-toxin genes.

Venom gland morphology in Pepsis pallidolimbata pallidolimbata and biological use and activity of Pepsis venom

1997 ◽  
Vol 75 (7) ◽  
pp. 1014-1019 ◽  
Author(s):  
E. Schoeters ◽  
J. Billen ◽  
J. O. Schmidt
Keyword(s):  
Venom Gland ◽  
Social Wasps ◽  
Morphological Organization ◽  
The Social ◽  
The Family ◽  
Venom Glands ◽  
Glandular Structures ◽  
Sibling Family

Spider wasps, i.e., the family Pompilidae, in general, and those belonging to the genus Pepsis in particular, are acknowledged to possess venoms that are algogenic to humans and thus have the parsimonious functions of causing paralysis and providing defense against predators. The morphological organization of the venom system and its complex convoluted gland closely resembles that in social members of the Vespidae. These features distinguish the venom glands of the Pompilidae from those of the sibling family Mutillidae as well as those of the family Sphecidae, which lack convoluted glands. Although the venom glands in Pepsis species are very similar in morphology to those of social vespids, the lethality of Pepsis venom to mammals is several times less than that of the social common wasps. These findings suggest that in terms of the evolution of venom activity and the associated glandular structures, there was apparently no need for social wasps to develop extra parts of the venom system for producing toxic, lethal, or powerful algogenic components. All of the glandular parts of the venom gland of social wasps were already present in pompilids (and eumenids) and, presumably, in their ancestors.

Histochemical Distribution of 5-Nucleotidase in Snake Tissues: Presence of 5-Nucleotidase and Absence of Alkaline Phosphomonoesterase in Venom Glands of the Rattlesnake

1952 ◽  
Vol s3-93 (24) ◽  
pp. 391-394
Author(s):  
D. E. BRAGDON ◽  
J.F. A. MCMANUS
Keyword(s):  
Alkaline Phosphatase ◽  
Smooth Muscle ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Venom Gland ◽  
Specific Alkaline Phosphatase ◽  
Rattlesnake Venom ◽  
Great Vessels ◽  
Venom Glands ◽  
Thyroid Epithelium

1. Activity of the specific alkaline phosphatase, 5-nucleotidase, is intense in the epithelium and secretion of the rattlesnake venom gland. Non-specific alkaline phosphatase activity is lacking. 2. Thyroid epithelium, the smooth muscle of great vessels, and (inconstantly) smooth muscle of abdominal hollow viscera show greater 5-nucleotidase than nonspecific activity. 3. These findings confirm the specificity of 5-nucleotidase.

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 Convergent evolution of venom gland transcriptomes across Metazoa

2021 ◽  
Author(s):  
Giulia Zancolli ◽  
Maarten Reijnders ◽  
Robert Waterhouse ◽  
Marc Robinson-Rechavi
Keyword(s):  
Gene Expression ◽  
Regulatory Networks ◽  
Molecular Mechanisms ◽  
Expression Profiles ◽  
Gene Expression Profiles ◽  
Venom Gland ◽  
Bioactive Molecules ◽  
Specific Gene ◽  
Animal Kingdom ◽  
Venom Glands

Animals have repeatedly evolved specialized organs and anatomical structures to produce and deliver a cocktail of potent bioactive molecules to subdue prey or predators: venom. This makes it one of the most widespread convergent functions in the animal kingdom. Whether animals have adopted the same genetic toolkit to evolved venom systems is a fascinating question that still eludes us. Here, we performed the first comparative analysis of venom gland transcriptomes from 20 venomous species spanning the main Metazoan lineages, to test whether different animals have independently adopted similar molecular mechanisms to perform the same function. We found a strong convergence in gene expression profiles, with venom glands being more similar to each other than to any other tissue from the same species, and their differences closely mirroring the species phylogeny. Although venom glands secrete some of the fastest evolving molecules (toxins), their gene expression does not evolve faster than evolutionarily older tissues. We found 15 venom gland specific gene modules enriched in endoplasmic reticulum stress and unfolded protein response pathways, indicating that animals have independently adopted stress response mechanisms to cope with mass production of toxins. This, in turns, activates regulatory networks for epithelial development, cell turnover and maintenance which seem composed of both convergent and lineage-specific factors, possibly reflecting the different developmental origins of venom glands. This study represents the first step towards an understanding of the molecular mechanisms underlying the repeated evolution of one of the most successful adaptive traits in the animal kingdom.

scholarly journals Peptide toxin blockers of voltage-sensitive K+ channels: inotropic effects on diaphragm

1999 ◽  
Vol 86 (3) ◽  
pp. 1009-1016 ◽  
Author(s):  
Erik van Lunteren ◽  
Michelle Moyer
Keyword(s):  
Inotropic Effects ◽  
Twitch Force ◽  
Voltage Gated ◽  
Blocking Voltage ◽  
Peptide Toxin ◽  
Peptide Toxins ◽  
Diaphragm In Vitro ◽  
Initial Force ◽  
Train Stimulation

Agents that block many types of K+ channels (e.g., the aminopyridines) have substantial inotropic effects in skeletal muscle. Specific blockers of ATP-sensitive and Ca2+-activated K+ channels, on the other hand, do not, or minimally, alter the force of nonfatigued muscle, consistent with a predominant role for voltage-gated K+ channels in regulating muscle force. To test this more directly, we examined the effects of peptide toxins, which in other tissues specifically block voltage-gated K+ channels, on rat diaphragm in vitro. Twitch force was increased in response to α-, β-, and γ-dendrotoxin and tityustoxin Kα (17 ± 6, 22 ± 5, 42 ± 14, and 13 ± 5%; P < 0.05, < 0.01, < 0.05, < 0.05, respectively) but not in response to δ-dendrotoxin or BSA (in which toxins were dissolved). Force during 20-Hz stimulation was also increased significantly by α-, β-, and γ-dendrotoxin and tityustoxin Kα. Among agents, increases in twitch force correlated with the degree to which contraction time was prolonged ( r = 0.88, P < 0.02). To determine whether inotropic effects could be maintained during repeated contractions, muscle strips underwent intermittent 20-Hz train stimulation for a duration of 2 min in presence or absence of γ-dendrotoxin. Force was significantly greater with than without γ-dendrotoxin during repetitive stimulation for the first 60 s of repetitive contractions. Despite the ∼55% higher value for initial force in the presence vs. absence of γ-dendrotoxin, the rate at which fatigue occurred was not accelerated by the toxin, as assessed by the amount of time over which force declined by 25 and 50%. These data suggest that blocking voltage-activated K+ channels may be a useful therapeutic strategy for augmenting diaphragm force, provided less toxic blockers of these channels can be found.

Inhibition of CFTR channels by a peptide toxin of scorpion venom

2004 ◽  
Vol 287 (5) ◽  
pp. C1328-C1341 ◽  
Author(s):  
Matthew D. Fuller ◽  
Zhi-Ren Zhang ◽  
Guiying Cui ◽  
Julia Kubanek ◽  
Nael A. McCarty
Keyword(s):  
Cystic Fibrosis ◽  
Single Channel ◽  
Genetic Disorders ◽  
Scorpion Venom ◽  
Burst Duration ◽  
Open Probability ◽  
Independent Manner ◽  
Peptide Toxin ◽  
Peptide Toxins ◽  
Block Mechanism

Peptide toxins have been valuable probes in efforts to identify amino acid residues that line the permeation pathway of cation-selective channels. However, no peptide toxins have been identified that interact with known anion-selective channels such as the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR channels are expressed in epithelial cells and are associated with several genetic disorders, including cystic fibrosis and polycystic kidney disease. Several organic inhibitors have been used to investigate the structure of the Cl− permeation pathway in CFTR. However, investigations of the wider cytoplasmic vestibule have been hindered by the lack of a high-affinity blocker that interacts with residues in this area. In this study we show that venom of the scorpion Leiurus quinquestriatus hebraeus reversibly inhibits CFTR, in a voltage-independent manner, by decreasing single-channel mean burst duration and open probability only when applied to the cytoplasmic surface of phosphorylated channels. Venom was able to decrease burst duration and open probability even when CFTR channels were locked open by treatment with either vanadate or adenosine 5′-(β,γ-imido)triphosphate, and block was strengthened on reduction of extracellular Cl− concentration, suggesting inhibition by a pore-block mechanism. Venom had no effect on ATP-dependent macroscopic opening rate in channels studied by inside-out macropatches. Interestingly, the inhibitory activity was abolished by proteinase treatment. We conclude that a peptide toxin contained in the scorpion venom inhibits CFTR channels by a pore-block mechanism; these experiments provide the first step toward isolation of the active component, which would be highly valuable as a probe for CFTR structure and function.

scholarly journals Molecular Cloning and Sequence Analysis of the cDNAs Encoding Toxin-Like Peptides from the Venom Glands of Tarantula Grammostola rosea

2012 ◽  
Vol 2012 ◽  
pp. 1-10 ◽  
Author(s):  
Tadashi Kimura ◽  
Seigo Ono ◽  
Tai Kubo
Keyword(s):  
Sequence Analysis ◽  
Molecular Cloning ◽  
Real Time ◽  
Cdna Library ◽  
Real Time Pcr ◽  
Bioactive Peptides ◽  
Venom Gland ◽  
Unique Peptide ◽  
Cdna Sequences ◽  
Venom Glands

Tarantula venom glands produce a large variety of bioactive peptides. Here we present the identification of venom components obtained by sequencing clones isolated from a cDNA library prepared from the venom glands of the Chilean common tarantula, Grammostola rosea. The cDNA sequences of about 1500 clones out of 4000 clones were analyzed after selection using several criteria. Forty-eight novel toxin-like peptides (GTx1 to GTx7, and GTx-TCTP and GTx-CRISP) were predicted from the nucleotide sequences. Among these peptides, twenty-four toxins are ICK motif peptides, eleven peptides are MIT1-like peptides, and seven are ESTX-like peptides. Peptides similar to JZTX-64, aptotoxin, CRISP, or TCTP are also obtained. GTx3 series possess a cysteine framework that is conserved among vertebrate MIT1, Bv8, prokineticins, and invertebrate astakines. GTx-CRISP is the first CRISP-like protein identified from the arthropod venom. Real-time PCR revealed that the transcripts for TCTP-like peptide are expressed in both the pereopodal muscle and the venom gland. Furthermore, a unique peptide GTx7-1, whose signal and prepro sequences are essentially identical to those of HaTx1, was obtained.

scholarly journals Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous Scorpion Centruroides limpidus (Karsch, 1879)

Toxins ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 247 ◽  
Author(s):  
Jimena I. Cid-Uribe ◽  
Erika P. Meneses ◽  
Cesar V. F. Batista ◽  
Ernesto Ortiz ◽  
Lourival D. Possani
Keyword(s):  
Ion Channel ◽  
High Throughput Sequencing ◽  
Venom Gland ◽  
K Channel ◽  
Rna Seq ◽  
Illumina Platform ◽  
Host Defense Peptides ◽  
Venom Glands ◽  
Mass Spectometry ◽  
First Time

Venom glands and soluble venom from the Mexican scorpion Centruroides limpidus (Karsch, 1879) were used for transcriptomic and proteomic analyses, respectively. An RNA-seq was performed by high-throughput sequencing with the Illumina platform. Approximately 80 million reads were obtained and assembled into 198,662 putative transcripts, of which 11,058 were annotated by similarity to sequences from available databases. A total of 192 venom-related sequences were identified, including Na+ and K+ channel-acting toxins, enzymes, host defense peptides, and other venom components. The most diverse transcripts were those potentially coding for ion channel-acting toxins, mainly those active on Na+ channels (NaScTx). Sequences corresponding to β- scorpion toxins active of K+ channels (KScTx) and λ-KScTx are here reported for the first time for a scorpion of the genus Centruroides. Mass fingerprint corroborated that NaScTx are the most abundant components in this venom. Liquid chromatography coupled to mass spectometry (LC-MS/MS) allowed the identification of 46 peptides matching sequences encoded in the transcriptome, confirming their expression in the venom. This study corroborates that, in the venom of toxic buthid scorpions, the more abundant and diverse components are ion channel-acting toxins, mainly NaScTx, while they lack the HDP diversity previously demonstrated for the non-buthid scorpions. The highly abundant and diverse antareases explain the pancreatitis observed after envenomation by this species.

scholarly journals Production and packaging of a biological arsenal: Evolution of centipede venoms under morphological constraint

2015 ◽  
Vol 112 (13) ◽  
pp. 4026-4031 ◽  
Author(s):  
Eivind A. B. Undheim ◽  
Brett R. Hamilton ◽  
Nyoman D. Kurniawan ◽  
Greg Bowlay ◽  
Bronwen W. Cribb ◽  
...  
Keyword(s):  
Prey Capture ◽  
Imaging Mass Spectrometry ◽  
Venom Gland ◽  
Toxin Production ◽  
Current Data ◽  
Secretory Cells ◽  
Physical Damage ◽  
Venom Glands ◽  
Protein Toxins ◽  
Morphological Constraint

Venom represents one of the most extreme manifestations of a chemical arms race. Venoms are complex biochemical arsenals, often containing hundreds to thousands of unique protein toxins. Despite their utility for prey capture, venoms are energetically expensive commodities, and consequently it is hypothesized that venom complexity is inversely related to the capacity of a venomous animal to physically subdue prey. Centipedes, one of the oldest yet least-studied venomous lineages, appear to defy this rule. Although scutigeromorph centipedes produce less complex venom than those secreted by scolopendrid centipedes, they appear to rely heavily on venom for prey capture. We show that the venom glands are large and well developed in both scutigerid and scolopendrid species, but that scutigerid forcipules lack the adaptations that allow scolopendrids to inflict physical damage on prey and predators. Moreover, we reveal that scolopendrid venom glands have evolved to accommodate a much larger number of secretory cells and, by using imaging mass spectrometry, we demonstrate that toxin production is heterogeneous across these secretory units. We propose that the differences in venom complexity between centipede orders are largely a result of morphological restrictions of the venom gland, and consequently there is a strong correlation between the morphological and biochemical complexity of this unique venom system. The current data add to the growing body of evidence that toxins are not expressed in a spatially homogenous manner within venom glands, and they suggest that the link between ecology and toxin evolution is more complex than previously thought.

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