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The chelicerae of the three major lineages within Araneae. The abstract ventral sides illustrate the different chelicerae configurations and major traits are plotted on the phylogram. Solifugae are added as an older chelicerate group that still feature the more ancient (plesiomorphic) state of chelicerae, which were originally three-segmented and scissor-like.
Source publication
Spiders are diverse, predatory arthropods that have inhabited Earth for around 400 million years. They are well known for their complex venom systems that are used to overpower their prey. Spider venoms contain many proteins and pep-tides with highly specific and potent activities suitable for biomedical or agrochemical applications, but the key ro...
Context in source publication
Context 1
... venom system of spiders is organized around the chelicerae, which differ in organization according to the lineage: while Mesothelae and Mygalomorphae possess chelicerae that are orthognathous (chelae in parallel orientation), the araneomorphs evolved chelicerae that are labidognathous (chelae are facing each other) as illustrated in Fig. 2. In spiders, the chelicerae feature two functional units that move in a jack-knife fashion. The first unit, a basal segment, is attached to the prosoma and forms a mobile base for the second unit, a ...
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Citations
... Animal venoms provide a remarkably abundant and diverse source of unique proteins and peptides, many with medically-relevant activities (Saez et al., 2010;Herzig et al., 2020;Bordon et al., 2020). Venomous animals have recruited many different toxins, which are used to capture prey, to facilitate feeding, for intraspecific competition and to deter predators (Schendel et al., 2019;Lüddecke et al., 2022). A particularly rich source of biomolecules is found in spiders. ...
... More recent analysis of venoms from the wandering RTA-clade spiders have revealed a variety of cytolytic peptides also known as cationic peptides, short linear peptides or spider venom antimicrobial peptides (AMPs) (Yan and Adams, 1998;Vassilevski et al., 2009;Trachsel et al., 2012;Dubovskii et al., 2015;Tang et al., 2020;Kuhn-Nentwig et al., 2021;Lüddecke et al., 2022). They usually contain 15-35 amino acids, form α-helices with a hydrophobic face, and are positively charged. ...
... Short linear peptides from spider venoms are thought to promote the uptake of co-injected venom components, suggesting trophic functions or roles to deter predators, and this has been confirmed for several peptides Lüddecke et al., 2022). However, the recent analysis of four LS-AMP families does not support such trophic functions, and suggests instead the principal role may be to suppress the growth of bacteria in the venom glands (Tan et al., 2022;Lüddecke et al., 2023a). ...
Spider-derived peptides with insecticidal, antimicrobial and/or cytolytic activities, also known as spider venom antimicrobial peptides (AMPs), can be found in the venoms of RTA-clade spiders. They show translational potential as therapeutic leads. A set of 52 AMPs has been described in the Chinese wolf spider (Lycosa shansia), and many have been shown to exhibit antibacterial effects. Here we explored the potential to enhance their antimicrobial activity using bioengineering. We generated a panel of artificial derivatives of an A-family peptide and screened their activity against selected microbial pathogens, vertebrate cells and insects. In several cases, we increased the antimicrobial activity of the derivatives while retaining the low cytotoxicity of the parental molecule. Furthermore, we injected the peptides into adult Drosophila suzukii and found no evidence of insecticidal effects, confirming the low levels of toxicity. Our data therefore suggest that spider venom linear peptides naturally defend the venom gland against microbial colonization and can be modified into more potent antimicrobial agents that could help to battle infectious diseases in the future.
... The evolution of epidermal glands into more complex glands has been reported for several hexapods [86] and co-option of nonspecialised into functionally specialised glands appears to be a widespread phenomenon across animals. For example, the venom glands of some arthropods [42,[87][88][89][90][91][92][93], snakes [94], spiders [95], leeches [96,97], cephalopods [98,99] and even mammals [100] turned out to have evolved from salivary glands, and salt-secreting glands in tetrapods appear to have evolved from non-salt-secreting glands [101]. ...
Background
Evolution of novelty is a central theme in evolutionary biology, yet studying the origins of traits with an apparently discontinuous origin remains a major challenge. Venom systems are a well-suited model for the study of this phenomenon because they capture several aspects of novelty across multiple levels of biological complexity. However, while there is some knowledge on the evolution of individual toxins, not much is known about the evolution of venom systems as a whole. One way of shedding light on the evolution of new traits is to investigate less specialised serial homologues, i.e. repeated traits in an organism that share a developmental origin. This approach can be particularly informative in animals with repetitive body segments, such as centipedes.
Results
Here, we investigate morphological and biochemical aspects of the defensive telopodal glandular organs borne on the posterior legs of venomous stone centipedes (Lithobiomorpha), using a multimethod approach, including behavioural observations, comparative morphology, proteomics, comparative transcriptomics and molecular phylogenetics. We show that the anterior venom system and posterior telopodal defence system are functionally convergent serial homologues, where one (telopodal defence) represents a model for the putative early evolutionary state of the other (venom). Venom glands and telopodal glandular organs appear to have evolved from the same type of epidermal gland (four-cell recto-canal type) and while the telopodal defensive secretion shares a great degree of compositional overlap with centipede venoms in general, these similarities arose predominantly through convergent recruitment of distantly related toxin-like components. Both systems are composed of elements predisposed to functional innovation across levels of biological complexity that range from proteins to glands, demonstrating clear parallels between molecular and morphological traits in the properties that facilitate the evolution of novelty.
Conclusions
The evolution of the lithobiomorph telopodal defence system provides indirect empirical support for the plausibility of the hypothesised evolutionary origin of the centipede venom system, which occurred through functional innovation and gradual specialisation of existing epidermal glands. Our results thus exemplify how continuous transformation and functional innovation can drive the apparent discontinuous emergence of novelties on higher levels of biological complexity.
... 19,[26][27][28] This combination of chemical diversity and powerful pharmacology suggests that arachnids may be the most promising venom-based source of biomedical innovation, including the field of antimicrobial drugs. 29 Despite the promise of arachnid venoms, few toxins have been isolated and an even smaller number has been functionally characterized. 21,30,31 This reflects an anthropocentric bias toward larger and potentially more dangerous species, especially those in which venom is easier to access. ...
... 39 Their venom contains several putative neurotoxic peptides that probably interfere with voltage-gated potassium and sodium channels. 29,40,54 Trophic venom must induce rapid effects to ensure immediate prey paralysis, and these neurotoxic peptides are likely to fulfill such a function. In contrast, checacin 1 and its derivatives showed insecticidal activity in aphid feeding assays, but only after 72 h. ...
... Lastly, arachnid toxins are known to often exert synergistic activities, and thus combinatorial assays may be required to fully unveil the bioactivity spectrum of arachnid toxins. 29 As of yet, this aspect is fully unstudied for pseudoscorpion toxins, and future works should perform bioactivity assays with combinations of checacin toxins. ...
Arthropod venoms contain bioactive molecules attractive for biomedical applications. However, few of these have been isolated, and only a tiny number has been characterized. Pseudoscorpions are small arachnids whose venom has been largely overlooked. Here, we present the first structural and functional assessment of the checacin toxin family, discovered in the venom of the house pseudoscorpion (Chelifer cancroides). We combined in silico and in vitro analyses to establish their bioactivity profile against mi- crobes and various cell lines. This revealed inhibitory effects against bacteria and fungi. We observed cyto- toxicity against specific cell types and effects involving second messengers. Our work provides insight into the biomedical potential and evolution of pseudoscorpion venoms. We propose that plesiotypic che- cacins evolved to defend the venom gland against infection, whereas apotypic descendants evolved additional functions. Our work highlights the importance of considering small and neglected species in biodiscovery programs.
... Gene duplication and adaptive selection are thought to be the main drivers of venom evolution [72,73]. Venom genes expand to form the gene family that can coexpress and lead to a significant increase in expression level. ...
Venom plays a crucial role in the defense and predation of venomous animals. Spiders (Araneae) are among the most successful predators and have a fascinating venom composition. Their venom mainly contains disulfide-rich peptides and large proteins. Here, we analyzed spider venom protein families, utilizing transcriptomic and genomic data, and highlighted their similarities and differences. We show that spiders have specific combinations of toxins for better predation and defense, typically comprising a core toxin expressed alongside several auxiliary toxins. Among them, the CAP superfamily is widely distributed and highly expressed in web-building Araneoidea spiders. Our analysis of evolutionary relationships revealed four subfamilies (subA-subD) of the CAP superfamily that differ in structure and potential functions. CAP proteins are composed of a conserved CAP domain and diverse C-terminal domains. CAP subC shares similar domains with the snake ion channel regulator svCRISP proteins, while CAP subD possesses a sequence similar to that of insect venom allergen 5 (Ag5). Furthermore, we show that gene duplication and selective expression lead to increased expression of CAP subD, making it a core member of the CAP superfamily. This study sheds light on the functional diversity of CAP subfamilies and their evolutionary history, which has important implications for fully understanding the composition of spider venom proteins and the core toxin components of web-building spiders.
... The chemical characterization of spider toxins explains venom toxicity and potential effects on humans and animals. More than 3000 different molecules have been characterized (Lüddecke et al. 2022 ), encompassing inorganic salts, nucleotides, free amino acids, polyamines, neurotransmitters, peptides, and proteins (Escoubas and Rash 2004, Macedo et al. 2021, Lüddecke et al. 2022 ). Among spider venoms, those from Theraphosidae family are well studied; Lüddecke et al. ( 2019 ) estimated that 28% of known spider toxin sequences deposited in public databases belong to members of this family. ...
... The chemical characterization of spider toxins explains venom toxicity and potential effects on humans and animals. More than 3000 different molecules have been characterized (Lüddecke et al. 2022 ), encompassing inorganic salts, nucleotides, free amino acids, polyamines, neurotransmitters, peptides, and proteins (Escoubas and Rash 2004, Macedo et al. 2021, Lüddecke et al. 2022 ). Among spider venoms, those from Theraphosidae family are well studied; Lüddecke et al. ( 2019 ) estimated that 28% of known spider toxin sequences deposited in public databases belong to members of this family. ...
Aim
Tarantulas are one of the largest predatory arthropods in tropical regions. Tarantulas though not lethal to humans, their venomous bite kills small animals and insect upon which they prey. To understand the abiotic and biotic components involved in Neotropical tarantula bites, we conducted a venom-microbiomics study in eight species from Costa Rica.
Methods and results
We determined that the toxin profiles of tarantula venom are highly diverse using shotgun proteomics; the most frequently encountered toxins were ω-Ap2 toxin, neprilysin-1, and several teraphotoxins. Through culture-independent and culture-dependent methods, we determined the microbiota present in the venom and excreta to evaluate the presence of pathogens that could contribute to primary infections in animals, including humans. The presence of opportunistic pathogens with hemolytic activity was observed, with a prominence of Stenotrophomonas in the venoms. Other bacteria found in venoms and excreta with hemolytic activity included members of the genera Serratia, Bacillus, Acinetobacter, Microbacterium, and Morganella.
Conclusions
Our data shed light on the venom- and gut-microbiome associated with Neotropical tarantulas. This information may be useful for treating bites from these arthropods in both humans and farm animals, while also providing insight into the toxins and biodiversity of this little-explored microenvironment.
... Animal venoms provide a remarkably abundant and diverse source of unique proteins and peptides, many with medically-relevant activities [1][2][3].Venomous animals have recruited many different toxins, which are used to capture prey, to facilitate feeding, for intraspecific competition and to deter predators [4,5]. A particularly rich source of biomolecules is found in spiders which have the potential to yield ~10 million unique toxins. ...
... More recent analysis of venoms from the wandering RTA-clade spiders have revealed a variety of cytolytic peptides also known as cationic peptides, short linear peptides or spider venom antimicrobial peptides (AMPs) [4,[8][9][10][11][12][13][14]. They usually contain 15-35 amino acids, form α -helices with a hydrophobic face, and are positively charged. ...
... Short linear peptides from spider venoms are thought to promote the uptake of co-injected venom components, suggesting trophic functions or roles to deter predators, and this has been confirmed for several peptides [4,34]. However, the recent analysis of four LS-AMP families does not support such trophic functions, and suggests instead the principal role may be to suppress the growth of bacteria in the venom glands [24,25]. ...
Peptides with insecticidal, antimicrobial and/or cytolytic activities, also known as spider venom antimicrobial peptides (AMPs), can be found in the venoms of RTA-clade spiders. They show translational potential as therapeutic leads. A set of 52 AMPs has been described in the Chinese wolf spider (Lycosa shansia), and many have been shown to exhibit antibacterial effects. Here we explored the potential to enhance their antimicrobial activity using bioengineering. We generated a panel of artificial derivatives of an A-family peptide and screened their activity against selected microbial pathogens, vertebrate cells and insects. In several cases, we increased the antimicrobial activity of the derivatives while retaining the low cytotoxicity of the parental molecule. Furthermore, we injected the peptides into adult Drosophila suzukii and found no evidence of insecticidal effects, confirming the low levels of toxicity. Our data therefore suggest that spider venom linear peptides can be modified into more potent antimicrobial agents that could help to battle infectious diseases in the future.
... Uloboridae spiders are considered evolutionarily less advanced as they have lost their venom glands and, thus, they rely more heavily on their webs to seize and immobilize their prey. Spiders need to fully wrap insects, their main prey, in their webs in order to immobilize them [19]. ...
... Spider venoms encompass numerous proteins and peptides with remarkably specific and potent characteristics. This innovation has played a pivotal role in enabling spiders to thrive and emerge as one of the most successful animal lineages (e.g., Agnarsson et al. 2013;Santos et al. 2017;Lüddecke et al. 2021). In many cases, these toxins can be medical importance to humans. ...
Wandering spiders (genus Phoneutria) hold a prominent position as some of the world's most medically significant venomous arachnids, especially in Brazil. In this study, we record and illustrate for the first time, the Darwin wasp Camera thoracica (Szépligeti, 1916) as a natural enemy of the ctenid Phoneutria nigriventer (Keyserling, 1891). Furthermore, we provide a description of the previously unknown male wasp, update and standardize the description of the female, and provide biological notes.
... The ability to produce a venom, a mix of molecules used to disrupt the normal physiological processes in another organism [1], is a trait that evolved independently over 101 times across the animal kingdom [2], leading to a total of more than 200 000 described venomous species on Earth [2]. Since each species is able to produce from a few tens to a few hundreds of unique toxins [3][4][5], venomous organisms represent a fantastic reservoir of millions of toxins. Some of these organisms also represent a serious threat for human health: snakes only are responsible for more than 100 000 casualties per year [6], and developing effective and specific antivenoms is thus a critical task in venom research. ...
Venomous organisms have independently evolved the ability to produce toxins 101 times during their evolutionary history, resulting in over 200 000 venomous species. Collectively, these species produce millions of toxins, making them a valuable resource for bioprospecting and understanding the evolutionary mechanisms underlying genetic diversification. RNA-seq is the preferred method for characterizing toxin repertoires, but the analysis of the resulting data remains challenging. While early approaches relied on similarity-based mapping to known toxin databases, recent studies have highlighted the importance of structural features for toxin detection. The few existing pipelines lack an integration between these complementary approaches, and tend to be difficult to run for non-experienced users. To address these issues, we developed DeTox, a comprehensive and user-friendly tool for toxin research. It combines fast execution, parallelization and customization of parameters. DeTox was tested on published transcriptomes from gastropod mollusks, cnidarians and snakes, retrieving most putative toxins from the original articles and identifying additional peptides as potential toxins to be confirmed through manual annotation and eventually proteomic analysis. By integrating a structure-based search with similarity-based approaches, DeTox allows the comprehensive characterization of toxin repertoire in poorly-known taxa. The effect of the taxonomic bias in existing databases is minimized in DeTox, as mirrored in the detection of unique and divergent toxins that would have been overlooked by similarity-based methods. DeTox streamlines toxin annotation, providing a valuable tool for efficient identification of venom components that will enhance venom research in neglected taxa.
... Peptides are a promising candidate for next-generation drugs due to their molecular flexibility and ability to target multiple molecules [47]. Among venomous organisms, the spider is known as the taxon with the highest diversity of toxin peptides [48,49]. In particular, the venom components of spiders belonging to the Loxosceles and Phoneutria genera are associated with anti-inflammatory properties [50]. ...
With the increasing challenge of controlling infectious diseases due to the emergence of antibiotic-resistant strains, the importance of discovering new antimicrobial agents is rapidly increasing. Animal venoms contain a variety of functional peptides, making them a promising platform for pharmaceutical development. In this study, a novel toxin peptide with antibacterial and anti-inflammatory activities was discovered from the spider venom gland transcriptome by implementing computational approaches. Lycotoxin-Pa2a (Lytx-Pa2a) showed homology to known-spider toxin, where functional prediction indicated the potential of both antibacterial and anti-inflammatory peptides without hemolytic activity. The colony-forming assay and minimum inhibitory concentration test showed that Lytx-Pa2a exhibited comparable or stronger antibacterial activity against pathogenic strains than melittin. Following mechanistic studies revealed that Lytx-Pa2a disrupts both cytoplasmic and outer membranes of bacteria while simultaneously inducing the accumulation of reactive oxygen species. The peptide exerted no significant toxicity when treated to human primary cells, murine macrophages, and bovine red blood cells. Moreover, Lytx-Pa2a alleviated lipopolysaccharide-induced inflammation in mouse macrophages by suppressing the expression of inflammatory mediators. These findings not only suggested that Lytx-Pa2a with dual activity can be utilized as a new antimicrobial agent for infectious diseases but also demonstrated the implementation of in silico methods for discovering a novel functional peptide, which may enhance the future utilization of biological resources.
