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Toxins
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Transcriptomic and Proteomic Study on Animal Venom: Looking Forward
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Transcriptomic and Proteomic Study on Animal Venom: Looking Forward

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: 30 September 2024 | Viewed by 1405

Special Issue Editor

Dr. Paulo Lee Ho

E-Mail Website
Guest Editor
BioIndustrial Center, Institute Butantan, São Paulo 05503-900, Brazil
Interests: snake venom; genomic; transcriptome; protein chemistry; antiserum production

Special Issue Information

Dear Colleagues,

Transcriptomic and proteomic studies concerning venom and venom glands constituted a major breakthrough in the characterization and knowledge of global crude venom compositions, and animal venom and venom glands in particular. More than 20 years have passed since the first studies utilized omics technologies, providing the first highthroughput data using these techniques. A critical evaluation of their contributions as well as their limitations may help to guide future research on animal venom toxin biology, with potential application in biomedical research. Novel technologies that can be combined with transcriptomic and proteomic studies are also emerging, providing new tools with the potential for a high impact in envenomation biology, evolution, therapy, the mechanisms implicated in the post-translational modification of these toxins and many other aspects. These would fill the knowledge gap at an accelerated pace. With this in mind, we will review the achievements, present contributions, gaps in the literature, integration and perspectives regarding these technologies for application in animal toxin biology and biomedical research, particularly when combined with new emerging technologies.

Dr. Paulo Lee Ho
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • transcriptome
  • proteome
  • venom composition
  • toxin(s)

Published Papers (2 papers)

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Research

19 pages, 10599 KiB  
Article
Identification and Evolutionary Analysis of the Widely Distributed CAP Superfamily in Spider Venom
by Hongcen Jiang, Yiru Wang, Guoqing Zhang, Anqiang Jia, Zhaoyuan Wei and Yi Wang
Toxins 2024, 16(6), 240; https://doi.org/10.3390/toxins16060240 - 24 May 2024
Viewed by 339
Abstract
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, [...] Read more.
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. Full article
(This article belongs to the Special Issue Transcriptomic and Proteomic Study on Animal Venom: Looking Forward)
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16 pages, 3236 KiB  
Article
Unveiling Novel Kunitz- and Waprin-Type Toxins in the Micrurus mipartitus Coral Snake Venom Gland: An In Silico Transcriptome Analysis
by Mónica Saldarriaga-Córdoba, Claudia Clavero-León, Paola Rey-Suarez, Vitelbina Nuñez-Rangel, Ruben Avendaño-Herrera, Stefany Solano-González and Juan F. Alzate
Toxins 2024, 16(5), 224; https://doi.org/10.3390/toxins16050224 - 11 May 2024
Viewed by 527
Abstract
Kunitz-type peptide expression has been described in the venom of snakes of the Viperidae, Elapidae and Colubridae families. This work aimed to identify these peptides in the venom gland transcriptome of the coral snake Micrurus mipartitus. Transcriptomic analysis revealed a high diversity [...] Read more.
Kunitz-type peptide expression has been described in the venom of snakes of the Viperidae, Elapidae and Colubridae families. This work aimed to identify these peptides in the venom gland transcriptome of the coral snake Micrurus mipartitus. Transcriptomic analysis revealed a high diversity of venom-associated Kunitz serine protease inhibitor proteins (KSPIs). A total of eight copies of KSPIs were predicted and grouped into four distinctive types, including short KSPI, long KSPI, Kunitz–Waprin (Ku-WAP) proteins, and a multi-domain Kunitz-type protein. From these, one short KSPI showed high identity with Micrurus tener and Austrelaps superbus. The long KSPI group exhibited similarity within the Micrurus genus and showed homology with various elapid snakes and even with the colubrid Pantherophis guttatus. A third group suggested the presence of Kunitz domains in addition to a whey-acidic-protein-type four-disulfide core domain. Finally, the fourth group corresponded to a transcript copy with a putative 511 amino acid protein, formerly annotated as KSPI, which UniProt classified as SPINT1. In conclusion, this study showed the diversity of Kunitz-type proteins expressed in the venom gland transcriptome of M. mipartitus. Full article
(This article belongs to the Special Issue Transcriptomic and Proteomic Study on Animal Venom: Looking Forward)
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