Physiological and biochemical characterization of egg extract of black widow spiders to uncover molecular basis of egg toxicity

Yan, Yizhong; Li, Jianjun; Zhang, Yiya; Xu, Peng; Guo, Tianyao; Wang, Jirong; Hu, Weijun; Duan, Zhigui; Wang, Xianchun

doi:10.1186/0717-6287-47-17

Cited by 13 publications

(15 citation statements)

References 41 publications

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“…Besides, analysis of cellular component indicated that the identified proteins were distributed in various parts of the cell, including the cell interior and the cell surface (Figure 1C). These data suggest that proteins identified through the transcriptome analysis are extensively distributed in various subcellular locations of the L. tredecimguttatus eggs and involved in multiple cellular processes and biological functions, particularly in binding, catalysis, development, etc., which is in agreement with the basic functions of the eggs and the results of our previous work [14,15]. …”

Section: Resultssupporting

confidence: 93%

“…In addition, the molecular weights of the proteins in eggs are mainly distributed in the range of from about 34 kDa to above 170 kDa, with the highest abundant protein bands at around 65 kDa and 130 kDa, respectively. Besides, Yan et al [14] studied the physiological and biochemical properties of the egg extract, and the results showed that the extract could completely block the neuromuscular transmission in mouse isolated phrenic nerve-hemidiaphragm preparations and inhibit the voltage-activated Na + , K + and Ca 2+ currents in rat DRG neurons. Furthermore, the neurotoxicity of the eggs to mammals was shown to be primarily attributed to their high-molecular-mass protein components.…”

Section: Resultsmentioning

confidence: 99%

“…For example, HWTX-XI from spider and Hg1 from scorpion are two Kunitz-type and bi-functional toxins because they are trypsin inhibitors as well as Kv1.1 and Kv1.3 potassium channel blockers, respectively [47,50,51]. In the eggs, there are 30 unigenes (Table S3) to encode serpins, of which five unigenes (comp10510_c0_seq1, comp199008_c0_seq1, comp191339_c0_seq1, comp31304_c0_seq2 and comp15360_c0_seq1) encode Kunitz-type serpins, suggesting that the inhibitory activity of the egg extract on voltage-gated ion channels especially potassium channels described by Yan et al [14] may involve these components.…”

Section: Resultsmentioning

confidence: 99%

“…L. tredecimguttatus spiders are highly poisonous and usually cause adverse reactions even lethal effects on humans and animals by envenomation [4], so ordinary people are afraid of the spiders while toxinologists are interested in them because all kinds of toxic components contained in poisonous spiders constitute a library of natural bioactive substances to discover and screen for pharmacological tool reagents, drug leads and insecticides [5,6,7]. As one of the most toxic spider species, the black widow spider differs from snake, scorpion and some other venomous spider species in that it has toxic components not only in its venomous glands [8,9,10,11] but also throughout its body, even in its newborn spiderlings and eggs [12,13,14]. Our research group has been using chromatography, proteomics, patch clamp and other related techniques to comprehensively analyze spider egg toxicity.…”

Section: Introductionmentioning

confidence: 99%

“…Our research group has been using chromatography, proteomics, patch clamp and other related techniques to comprehensively analyze spider egg toxicity. The results showed that the proteinaceous components in the egg extract are mainly high-molecular-mass proteins and the peptides below 5 kDa, and that the toxicity of the eggs are mainly due to the high-molecular-mass proteins [14,15]. Besides, three high-molecular-mass proteins and one low-molecular-mass peptide, named latroeggtoxin-I to latroeggtoxin-IV, respectively, were purified and characterized from the egg extract.…”

Section: Introductionmentioning

confidence: 99%

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Transcriptome Analysis to Understand the Toxicity of Latrodectus tredecimguttatus Eggs

Wang

2016

Toxins

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Latrodectus tredecimguttatus is a kind of highly venomous black widow spider, with toxicity coming from not only venomous glands but also other parts of its body as well as newborn spiderlings and eggs. Up to date, although L. tredecimguttatus eggs have been demonstrated to be rich in proteinaceous toxins, there is no systematic investigation on such active components at transcriptome level. In this study, we performed a high-throughput transcriptome sequencing of L. tredecimguttatus eggs with Illumina sequencing technology. As a result, 53,284 protein-coding unigenes were identified, of which 14,185 unigenes produced significant hits in the available databases, including 280 unigenes encoding proteins or peptides homologous to known proteinaceous toxins. GO term and KEGG pathway enrichment analyses of the 280 unigenes showed that 375 GO terms and 18 KEGG pathways were significantly enriched. Functional analysis indicated that these unigene-coded toxins have the bioactivities to degrade tissue proteins, inhibit ion channels, block neuromuscular transmission, provoke anaphylaxis, induce apoptosis and hyperalgesia, etc. No known typical proteinaceous toxins in L. tredecimguttatus venomous glands, such as latrotoxins, were identified, suggesting that the eggs have a different toxicity mechanism from that of the venom. Our present transcriptome analysis not only helps to reveal the gene expression profile and toxicity mechanism of the L. tredecimguttatus eggs, but also provides references for the further related researches.

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Section: Resultssupporting

confidence: 93%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Transcriptome Analysis to Understand the Toxicity of Latrodectus tredecimguttatus Eggs

Wang

2016

Toxins

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Structure–Function Relationship and Stability of Latroeggtoxin‐VI: A Proteinaceous Toxin From the Eggs of Latrodectus tredecimguttatus

Chen,

Sun,

Yin

et al. 2024

Peptide Science

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Latroeggtoxin‐VI (LETX‐VI), a peptide toxin discovered from the eggs of spider Latrodectus tredecimguttatus, was previously shown to promote the synthesis and release of dopamine in rat pheochromocytoma (PC12) cells, showing potential applications in the neurobiology and medicine. To further understand the structure and properties of LETX‐VI, the key residues were identified and their roles in the structure, function, and stability of LETX‐VI were analyzed in the present work. Based on the protein molecular docking, our previous work, and the relevant literature, the potential key residues of LETX‐VI were selected and identified by alanine‐scanning mutagenesis. The wild‐type LETX‐VI and its 13 mutants, including a double mutant, were prepared by gene cloning and heterologous expression in Escherichia coli, followed by activity, structure, and stability determination. The results demonstrated that the activity of the mutants K25A, R35A, K40A/R41A, and L45A, particularly R35A, to promote dopamine release from PC12 cells was significantly decreased compared with that of the wild‐type LETX‐VI, indicating that these mutated residues are the key residues. Circular dichroism (CD) analysis showed that the secondary structure of these mutants was not obviously different from that of wild‐type LETX‐VI, suggesting that mutation‐caused decrease in the activity of LETX‐VI is due to the changes in the binding site on the molecule surface, rather than the abnormal alternation of the molecular conformation of LETX‐VI. Acetonitrile (ACN) did not obviously influence the activity of LETX‐VI; however, 0.1% trifluoroacetic acid (TFA) treatment for 2 h significantly reduced its activity. Treatment with weakly acidic and basic buffers (pH ≥ 6.6) for 12 h was favorable for LETX‐VI and R35A to exert their activity. Higher temperatures (>37°C) decreased the activity of both wild‐type LETX‐VI and R35A. In conclusion, K25, R35, K40, R41, and L45 particularly R35 are the important functional site residues; during experiments, care should be taken to avoid the adverse influence of strong acid and high temperature on LETX‐VI. These observations have enhanced our understanding of the structure and properties of LETX‐VI and provided references for the subsequent modification of structure and function of LETX‐VI.

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Molecular basis and mechanism underlying the insecticidal activity of venoms and toxins from Latrodectus spiders

Wang

Tang

et al. 2018

Pest Management Science

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Latrodectus species are among the most venomous of spiders, with abundant toxic proteinaceous components in their venomous glands and other tissues, as well as their eggs. To date, several proteinaceous toxins with insecticidal potential, including α-insectotoxin and δ-insectotoxin, two of the most potent known insecticidal toxins, have been purified and characterized by comprehensively utilizing conventional biochemical techniques. This has greatly enhanced our knowledge of the molecular basis and mechanism of action of their toxicity. Application of proteomic and transcriptomic techniques further revealed the synergistic action of multiple Latrodectus proteinaceous toxins and toxin-like components. Insecticidal toxins from Latrodectus spiders have great potential in insect pest control; however, more studies are needed to further reveal their mechanisms of action and understand their structures and properties before any practical application, for example, the insecticidal toxin-containing fusion proteins with oral activity. Here, we review current knowledge of the molecular basis and mechanism of action underlying the insecticidal activity of venoms and toxins from Latrodectus spiders, and examine their potential application in insect pest control. © 2018 Society of Chemical Industry.

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Physiological and biochemical characterization of egg extract of black widow spiders to uncover molecular basis of egg toxicity

Cited by 13 publications

References 41 publications

Transcriptome Analysis to Understand the Toxicity of Latrodectus tredecimguttatus Eggs

Transcriptome Analysis to Understand the Toxicity of Latrodectus tredecimguttatus Eggs

Structure–Function Relationship and Stability of Latroeggtoxin‐VI: A Proteinaceous Toxin From the Eggs of Latrodectus tredecimguttatus

Molecular basis and mechanism underlying the insecticidal activity of venoms and toxins from Latrodectus spiders

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