-
Toxicon : Official Journal of the... Nov 2016This study characterized the protein/peptide profile of venom isolated from the spider Lasiodora sp. (Mygalomorphae, Theraphosidae) found in northeastern Brazil and...
This study characterized the protein/peptide profile of venom isolated from the spider Lasiodora sp. (Mygalomorphae, Theraphosidae) found in northeastern Brazil and determined its antimicrobial activity, toxicity against human cells, and hemolytic activity. Protein concentration of the Lasiodora sp. venom was 4.53 ± 0.38 mg/mL. SDS-PAGE showed proteins with molecular masses up to 75 kDa, some of which contained disulfide bridges. RP-HPLC analysis separate at least 12 peaks that were identified by mass spectrometry as peptides U-theraphotoxin-Lp1a (lasiotoxin-1), U-theraphotoxin-Lp1c (lasiotoxin-3), U-theraphotoxin-Lsp1a (LTx5), and ω-theraphotoxin-Asp3a as well as the proteins phospholipase A (PLA) and hyaluronidase. The crude venom exhibited bactericidal effect against Aeromonas sp., Bacillus subtilis, and Micrococcus luteus and fungicidal effect against Candida parapsilosis and Candida albicans. In addition, the venom exerted bacteriostatic effect against Klebsiella pneumoniae, Pseudomonas aeruginosa, and Staphylococcus aureus and fungistatic effect against Candida tropicalis and Candida krusei. The minimum inhibitory (MIC), minimum bactericidal (MBC), and minimum fungicidal (MFC) concentrations ranged from 3.9 to 500 μg/mL. The Lasiodora sp. venom decreased the viability of human peripheral blood mononuclear cells (PBMCs) by 50%-90% at concentrations of 0.1, 1, 10, and 100 μg/mL, promoting apoptosis of these cells. On the other hand, the venom showed weak hemolytic activity against Mus musculus erythrocytes (EC: 757 μg/mL). In conclusion, the Lasiodora sp. spider venom is a rich source of antimicrobial agents. Future studies will focus on identifying antimicrobial agents present in this venom and evaluating whether these agents contribute to its cytotoxic effects against PBMCs.
Topics: Animals; Anti-Infective Agents; Antineoplastic Agents; Hemolysis; Humans; Infant; Spider Venoms
PubMed: 27693304
DOI: 10.1016/j.toxicon.2016.09.019 -
Toxins Aug 2017Spider venoms are rich cocktails of bioactive peptides, proteins, and enzymes that are being intensively investigated over the years. In order to provide a better...
Spider venoms are rich cocktails of bioactive peptides, proteins, and enzymes that are being intensively investigated over the years. In order to provide a better comprehension of that richness, we propose a three-level family classification system for spider venom components. This classification is supported by an exhaustive set of 219 new profile hidden Markov models (HMMs) able to attribute a given peptide to its precise peptide type, family, and group. The proposed classification has the advantages of being totally independent from variable spider taxonomic names and can easily evolve. In addition to the new classifiers, we introduce and demonstrate the efficiency of , a new standalone tool that monitors HMM-based family classification and, after post-processing the result, reports the best classifier when multiple models produce significant scores towards given peptide queries. The combined used of and the new spider venom component-specific classifiers demonstrated 96% sensitivity to properly classify all known spider toxins from the UniProtKB database. These tools are timely regarding the important classification needs caused by the increasing number of peptides and proteins generated by transcriptomic projects.
Topics: Animals; Arthropod Proteins; Databases, Protein; Neurotoxins; Peptides; Proteomics; Spider Venoms; Spiders
PubMed: 28786958
DOI: 10.3390/toxins9080245 -
Toxins Apr 2022The transcriptome of the venom glands of the spider was analyzed using RNA-seq with an Illumina protocol, which yielded 86,424 assembled transcripts. A total of 682...
The transcriptome of the venom glands of the spider was analyzed using RNA-seq with an Illumina protocol, which yielded 86,424 assembled transcripts. A total of 682 transcripts were identified as potentially coding for venom components. Most of the transcripts found were neurotoxins (156) that commonly act on sodium and calcium channels. Nevertheless, transcripts coding for some enzymes (239), growth factors (48), clotting factors (6), and a diuretic hormone (1) were found, which have not been described in this spider genus. Furthermore, an enzymatic characterization of the venom of was performed, and the proteomic analysis showed a correlation between active protein bands and protein sequences found in the transcriptome. The transcriptomic analysis of venom glands show a deeper description of its protein components, allowing the identification of novel molecules that could lead to the treatment of human diseases, or could be models for developing bioinsecticides.
Topics: Animals; Colombia; Proteomics; Spider Venoms; Spiders; Transcriptome
PubMed: 35622542
DOI: 10.3390/toxins14050295 -
Toxins Oct 2017Beyond providing evolutionary advantages, venoms offer unique research tools, as they were developed to target functionally important proteins and pathways. As a key... (Review)
Review
Beyond providing evolutionary advantages, venoms offer unique research tools, as they were developed to target functionally important proteins and pathways. As a key pain receptor in the nociceptive pathway, transient receptor potential vanilloid 1 (TRPV1) of the TRP superfamily has been shown to be a target for several toxins, as a way of producing pain to deter predators. Importantly, TRPV1 is involved in thermoregulation, inflammation, and acute nociception. As such, toxins provide tools to understand TRPV1 activation and modulation, a critical step in advancing pain research and the development of novel analgesics. Indeed, the phytotoxin capsaicin, which is the spicy chemical in chili peppers, was invaluable in the original cloning and characterization of TRPV1. The unique properties of each subsequently characterized toxin have continued to advance our understanding of functional, structural, and biophysical characteristics of TRPV1. By building on previous reviews, this work aims to provide a comprehensive summary of the advancements made in TRPV1 research in recent years by employing animal toxins, in particular DkTx, RhTx, BmP01, toxins, APHCs and HCRG21. We examine each toxin's functional aspects, behavioral effects, and structural features, all of which have contributed to our current knowledge of TRPV1. We additionally discuss the key features of TRPV1's outer pore domain, which proves to be the target of the currently discussed toxins.
Topics: Animals; Scorpion Venoms; Sea Anemones; Snake Venoms; Spider Venoms; TRPV Cation Channels; Toxins, Biological
PubMed: 29035314
DOI: 10.3390/toxins9100326 -
Toxins Jan 2023Brown spider envenomation results in dermonecrosis, characterized by an intense inflammatory reaction. The principal toxins of brown spider venoms are phospholipase-D...
Brown spider envenomation results in dermonecrosis, characterized by an intense inflammatory reaction. The principal toxins of brown spider venoms are phospholipase-D isoforms, which interact with different cellular membrane components, degrade phospholipids, and generate bioactive mediators leading to harmful effects. The phospholipase D, LiRecDT1, possesses a loop that modulates the accessibility to the active site and plays a crucial role in substrate. In vitro and in silico analyses were performed to determine aspects of this enzyme's substrate preference. Sphingomyelin d18:1/6:0 was the preferred substrate of LiRecDT1 compared to other Sphingomyelins. Lysophosphatidylcholine 16:0/0:0 was preferred among other lysophosphatidylcholines, but much less than Sphingomyelin d18:1/6:0. In contrast, phosphatidylcholine d18:1/16:0 was not cleaved. Thus, the number of carbon atoms in the substrate plays a vital role in determining the optimal activity of this phospholipase-D. The presence of an amide group at C2 plays a key role in recognition and activity. In silico analyses indicated that a subsite containing the aromatic residues Y228 and W230 appears essential for choline recognition by cation-π interactions. These findings may help to explain why different cells, with different phospholipid fatty acid compositions exhibit distinct susceptibilities to brown spider venoms.
Topics: Animals; Sphingomyelins; Phosphoric Diester Hydrolases; Phospholipase D; Spider Venoms; Phospholipids; Lysophosphatidylcholines; Spiders
PubMed: 36828423
DOI: 10.3390/toxins15020109 -
Academic Emergency Medicine : Official... Feb 2011
Topics: Attitude of Health Personnel; Blood Transfusion; Child, Preschool; Emergency Service, Hospital; Fatal Outcome; Female; Hemolysis; Humans; Phosphoric Diester Hydrolases; Spider Bites; Spider Venoms
PubMed: 21314786
DOI: 10.1111/j.1553-2712.2010.00999.x -
Toxins Mar 2019Most knowledge of spider venom concerns neurotoxins acting on ion channels, whereas proteins and their significance for the envenomation process are neglected. The here...
Most knowledge of spider venom concerns neurotoxins acting on ion channels, whereas proteins and their significance for the envenomation process are neglected. The here presented comprehensive analysis of the venom gland transcriptome and proteome of focusses on proteins and cysteine-containing peptides and offers new insight into the structure and function of spider venom, here described as the dual prey-inactivation strategy. After venom injection, many enzymes and proteins, dominated by α-amylase, angiotensin-converting enzyme, and cysteine-rich secretory proteins, interact with main metabolic pathways, leading to a major disturbance of the cellular homeostasis. Hyaluronidase and cytolytic peptides destroy tissue and membranes, thus supporting the spread of other venom compounds. We detected 81 transcripts of neurotoxins from 13 peptide families, whereof two families comprise 93.7% of all cysteine-containing peptides. This raises the question of the importance of the other low-expressed peptide families. The identification of a venom gland-specific defensin-like peptide and an aga-toxin-like peptide in the hemocytes offers an important clue on the recruitment and neofunctionalization of body proteins and peptides as the origin of toxins.
Topics: Animals; Arthropod Proteins; Neurotoxins; Peptides; Predatory Behavior; Proteome; Spider Venoms; Spiders; Transcriptome
PubMed: 30893800
DOI: 10.3390/toxins11030167 -
Brazilian Journal of Medical and... Jul 2001Loxoscelism, the term used to describe lesions and clinical manifestations induced by brown spider's venom (Loxosceles genus), has attracted much attention over the last... (Review)
Review
Loxoscelism, the term used to describe lesions and clinical manifestations induced by brown spider's venom (Loxosceles genus), has attracted much attention over the last years. Brown spider bites have been reported to cause a local and acute inflammatory reaction that may evolve to dermonecrosis (a hallmark of envenomation) and hemorrhage at the bite site, besides systemic manifestations such as thrombocytopenia, disseminated intravascular coagulation, hemolysis, and renal failure. The molecular mechanisms by which Loxosceles venoms induce injury are currently under investigation. In this review, we focused on the latest reports describing the biological and physiopathological aspects of loxoscelism, with reference mainly to the proteases recently described as metalloproteases and serine proteases, as well as on the proteolytic effects triggered by L. intermedia venom upon extracellular matrix constituents such as fibronectin, fibrinogen, entactin and heparan sulfate proteoglycan, besides the disruptive activity of the venom on Engelbreth-Holm-Swarm basement membranes. Degradation of these extracellular matrix molecules and the observed disruption of basement membranes could be related to deleterious activities of the venom such as loss of vessel and glomerular integrity and spreading of the venom toxins to underlying tissues.
Topics: Animals; Basement Membrane; Extracellular Matrix; Hemostasis; Humans; Phosphoric Diester Hydrolases; Serine Endopeptidases; Spider Venoms; Spiders
PubMed: 11449301
DOI: 10.1590/s0100-879x2001000700002 -
ELife Feb 2023Spider venoms are a complex concoction of enzymes, polyamines, inorganic salts, and disulfide-rich peptides (DRPs). Although DRPs are widely distributed and abundant,...
Spider venoms are a complex concoction of enzymes, polyamines, inorganic salts, and disulfide-rich peptides (DRPs). Although DRPs are widely distributed and abundant, their bevolutionary origin has remained elusive. This knowledge gap stems from the extensive molecular divergence of DRPs and a lack of sequence and structural data from diverse lineages. By evaluating DRPs under a comprehensive phylogenetic, structural and evolutionary framework, we have not only identified 78 novel spider toxin superfamilies but also provided the first evidence for their common origin. We trace the origin of these toxin superfamilies to a primordial knot - which we name 'Adi Shakti', after the creator of the Universe according to Hindu mythology - 375 MYA in the common ancestor of Araneomorphae and Mygalomorphae. As the lineages under evaluation constitute nearly 60% of extant spiders, our findings provide fascinating insights into the early evolution and diversification of the spider venom arsenal. Reliance on a single molecular toxin scaffold by nearly all spiders is in complete contrast to most other venomous animals that have recruited into their venoms diverse toxins with independent origins. By comparatively evaluating the molecular evolutionary histories of araneomorph and mygalomorph spider venom toxins, we highlight their contrasting evolutionary diversification rates. Our results also suggest that venom deployment (e.g. prey capture or self-defense) influences evolutionary diversification of DRP toxin superfamilies.
Topics: Animals; Spider Venoms; Phylogeny; Disulfides; Peptides; Evolution, Molecular; Spiders
PubMed: 36757362
DOI: 10.7554/eLife.83761 -
Japanese Journal of Infectious Diseases Mar 2018The redback spider (Latrodectus hasseltii Thorell) reportedly invaded Japan in September 1995. To date, 84 redback spider bite cases have been reported; 7 of these cases...
The redback spider (Latrodectus hasseltii Thorell) reportedly invaded Japan in September 1995. To date, 84 redback spider bite cases have been reported; 7 of these cases employed the antivenom. Antivenom has been imported from Australia in the past, but because of restrictions on exportation it was evident that nearly all of the antivenom present in Japan would expire during 2014. In 2014, a plan was proposed to experimentally manufacture and stockpile a horse antiserum for ourselves, using redback spiders indigenous to Japan. A total of 11,403 female spiders were captured alive: 1,217 from the vicinity of Nishinomiya City, Hyogo prefecture, and 10,186 from Osaka prefecture. Of these, 10,007 females were dissected, and the venom was extracted from the venom glands of individuals and subjected to crude purification to yield 4 lots, of which the majority was α-latrotoxin. Among them, a large amount of single lots with an estimated protein content of 236 mg is subsequently scheduled to be used for immunizing horses. We also determined lethal toxicity of the venom (LD: 9.17 μg per mouse), and established the assay for the determination of an anti-lethal titer of antivenom in mice.
Topics: Animals; Antivenins; Female; Japan; Lethal Dose 50; Mice; Neutralization Tests; Spider Venoms; Spiders
PubMed: 29491237
DOI: 10.7883/yoken.JJID.2017.291