CAP superfamily proteins from venomous animals: Who we are and what to do?

Zhang, Qianqian; Xu, Jiawei; Zhou, Xi; Z, Liu

doi:10.1016/j.ijbiomac.2022.09.079

Cited by 8 publications

(7 citation statements)

References 86 publications

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“…In scorpions, their function in the venom remains unknown. However, about 119 coding transcripts have been reported in transcriptomic analyses, and their presence in venom has been verified in species of the Buthidae, Vaejovidae, Caraboctonidae, Superstitionidae, and Euscorpiidae families [ 18 , 33 , 63 ]. Seven coding transcripts with identity to CAP proteins were identified in this transcriptomic analysis, and three of them were found in the proteome ( Supplementary Tables S1 and S2 ).…”

Section: Resultsmentioning

confidence: 99%

Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the Scorpion Centruroides possanii (Buthidae) through Omic Technologies

García-Villalvazo

Jiménez-Vargas

Lino-López³

et al. 2023

Toxins

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Centruroides possanii is a recently discovered species of “striped scorpion” found in Mexico. Certain species of Centruroides are known to be toxic to mammals, leading to numerous cases of human intoxications in the country. Venom components are thought to possess therapeutic potential and/or biotechnological applications. Hence, obtaining and analyzing the secretory gland transcriptome and venom proteome of C. possanii is relevant, and that is what is described in this communication. Since this is a newly described species, first, its LD50 to mice was determined and estimated to be 659 ng/g mouse weight. Using RNA extracted from this species and preparing their corresponding cDNA fragments, a transcriptome analysis was obtained on a Genome Analyzer (Illumina) using the 76-base pair-end sequencing protocol. Via high-throughput sequencing, 19,158,736 reads were obtained and ensembled in 835,204 sequences. Of them, 28,399 transcripts were annotated with Pfam. A total of 244 complete transcripts were identified in the transcriptome of C. possanii. Of these, 109 sequences showed identity to toxins that act on ion channels, 47 enzymes, 17 protease inhibitors (PINs), 11 defense peptides (HDPs), and 60 in other components. In addition, a sample of the soluble venom obtained from this scorpion was analyzed using an Orbitrap Velos apparatus, which allowed for identification by liquid chromatography followed by mass spectrometry (LC-MS/MS) of 70 peptides and proteins: 23 toxins, 27 enzymes, 6 PINs, 3 HDPs, and 11 other components. Until now, this work has the highest number of scorpion venom components identified through omics technologies. The main novel findings described here were analyzed in comparison with the known data from the literature, and this process permitted some new insights in this field.

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Section: Resultsmentioning

confidence: 99%

Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the Scorpion Centruroides possanii (Buthidae) through Omic Technologies

García-Villalvazo

Jiménez-Vargas

Lino-López³

et al. 2023

Toxins

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“…The diversity and evolution of CRISPs in venomous animals is better described in snakes and terrestrial arthropods (like scorpions) than in mollusks. Even though they are believed to be relatively well conserved, only a few of these CAP domain-bearing proteins have been fully characterized (see Tadokoro et al, 2020;Zhang et al, 2022). It has been hypothesized that the evolution of CAP proteins (which started in bacteria) has been a multi-step process that potentially involved positive selection through nontoxin CRISPs and potentially from non-toxin to toxin (Vicens and Treviño, 2018;Tadokoro et al, 2020;Zhang et al, 2022).…”

Section: Discussionmentioning

confidence: 99%

“…Even though they are believed to be relatively well conserved, only a few of these CAP domain-bearing proteins have been fully characterized (see Tadokoro et al, 2020;Zhang et al, 2022). It has been hypothesized that the evolution of CAP proteins (which started in bacteria) has been a multi-step process that potentially involved positive selection through nontoxin CRISPs and potentially from non-toxin to toxin (Vicens and Treviño, 2018;Tadokoro et al, 2020;Zhang et al, 2022). This may explain a consider variability in sequence, structure and function of these proteins even with the same taxon.…”

Section: Discussionmentioning

confidence: 99%

“…Given the potential biological relevance of the toxin related transcripts CRVP, CTX and VIns (for details on these proteins see Ueda et al, 2008;De Meyts, 2016;Jiraćěk and Z ̌aḱova, 2019;Zhang et al, 2022), these were shortlisted for detailed analysis and validation. Predicting ORFs revealed that all bear different wellconserved domains (Figure 7A).…”

Section: Sepia Officinalis Express Toxin-encoding Transcripts Conserv...mentioning

confidence: 99%

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Transcriptome profiling of the posterior salivary glands of the cuttlefish Sepia officinalis from the Portuguese West coast

Gonçalves,

Moutinho Cabral,

Alves de Matos

et al. 2024

Front. Mar. Sci.

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Cephalopods like octopuses and cuttlefishes are known to secrete a ‘toxic saliva’ to inject into their prey, especially crustaceans since the XIX century. However, only in the mid-XX century were the first coleoid-specific toxins successfully isolated. Motivated by the growing interest on the global ocean as an almost inexhaustible source of novel bioactive compounds, we used RNA-Seq – based transcriptomics and de novo assembly of transcriptomes to screen the posterior salivary glands of Sepia officinalis (the common cuttlefish) from the Portuguese West coast for toxins and other bioactive proteins and peptides. Supported by microanatomical analyses, the posterior salivary glands constitute indeed the ‘venom gland’ whereas the more elusive anterior salivary glands (embedded in the buccal mass) are responsible for the production of mucin-rich saliva that is effectively the vehicle that transports the toxins as the venom is injected into the prey. Indeed, the transcriptomic profiling suggests that the cuttlefish venom is complex mixture of bioactive proteins, among which neurotoxins are major players, together with enzymes whose function is to digest the extracellular matrix to facilitate diffusion of the toxins. Nonetheless, by comparing with previous RNA-Seq data obtained from S. officinalis collected from other biogeographical areas, it may be suggested that significant inter-populational variation in venom composition can occur, which may potentially increase the span of bioactives secreted by these animals. We isolated and validated the full coding sequences for three important toxins, a cysteine-rich venom protein (CRVP), a venom insulin (VIns) and a cephalotoxin (CTX). The toxins seem to be relatively conserved among coleoids but diverging from other venomous mollusks such as cone snails. Their properties as potent modulators of glucose (in the case of VIns) and as potential neurotoxins (like CRVP and CTX) can render them primer targets for drug development.

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“…The CAP superfamily is a large venom protein family, also known as the cysteine-rich secretory proteins (CRISPs), antigen 5 (Ag5), and pathogenesis-related 1 (PR-1) superfamily, which is named after the first initials of the three proteins it includes [ 13 ]. This family is found in many venomous animals, such as reptiles (snakes [ 14 , 15 , 16 , 17 ], lizards [ 18 , 19 , 20 ]) and arthropods (bees [ 21 ], ants [ 22 ], spiders [ 23 , 24 , 25 , 26 ], scorpions [ 27 ]), as well as bacteria [ 28 ], plants [ 29 ], fungi [ 30 ], and mammals [ 31 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and Evolutionary Analysis of the Widely Distributed CAP Superfamily in Spider Venom

Jiang,

Wang,

Zhang

et al. 2024

Toxins

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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.

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CAP superfamily proteins from venomous animals: Who we are and what to do?

Cited by 8 publications

References 86 publications

Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the Scorpion Centruroides possanii (Buthidae) through Omic Technologies

Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the Scorpion Centruroides possanii (Buthidae) through Omic Technologies

Transcriptome profiling of the posterior salivary glands of the cuttlefish Sepia officinalis from the Portuguese West coast

Identification and Evolutionary Analysis of the Widely Distributed CAP Superfamily in Spider Venom

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