Unveiling Novel Kunitz- and Waprin-Type Toxins in the Micrurus mipartitus Coral Snake Venom Gland: An In Silico Transcriptome Analysis

Author:

Saldarriaga-Córdoba Mónica1ORCID,Clavero-León Claudia2ORCID,Rey-Suarez Paola3ORCID,Nuñez-Rangel Vitelbina34ORCID,Avendaño-Herrera Ruben5,Solano-González Stefany6ORCID,Alzate Juan F.7ORCID

Affiliation:

1. Escuela de Medicina Veterinaria, Universidad Bernardo O’Higgins, Santiago 8320000, Chile

2. Centro de Investigación en Recursos Naturales y Sustentabilidad (CIRENYS), Universidad Bernardo O’Higgins, Santiago 8320000, Chile

3. Grupo de Investigación en Toxinología, Alternativas Terapéuticas y Alimentarias, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia, Medellín 50010, Colombia

4. Escuela de Microbiología, Universidad de Antioquia, Medellín 50010, Colombia

5. Facultad de Ciencias de la Vida & Centro de Investigación Marina Quintay (CIMARQ), Universidad Andrés Bello, Viña del Mar 2531015, Chile

6. Laboratorio de Bioinformática Aplicada, Escuela de Ciencias Biológicas, Universidad Nacional, Heredia 86-3000, Costa Rica

7. Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad de Antioquia, Medellín 50010, Colombia

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 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.

Funder

Agencia Nacional de Investigación y Desarrollo

Publisher

MDPI AG

Reference83 articles.

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4. The gene structure and evolution of ku-wap-fusin (Kunitz Waprin Fusion Protein), a novel evolutionary intermediate of the Kunitz Serine Protease Inhibitors and Waprins from Sistrurus catenatus (Massasauga Rattlesnake) Venom Glands;Doley;Open Evol. J.,2010

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