| Autor: |
Lino-López GJ; Facultad de Ciencias Químicas, Universidad de Colima, 28400 Coquimatlan, Colima, México.; Departamento de Control Biológico, CNRF-DGSV-SENASICA-SADER, Km 1.5 Carretera Tecomán-Estación FFCC, Col. Tepeyac, 28110 Tecomán, Colima, México., Ruiz-May E; Instituto de Ecología, Carretera antigua a Coatepec 351, El Haya, 91073 Xalapa, Veracruz,México., Elizalde-Contreras JM; Instituto de Ecología, Carretera antigua a Coatepec 351, El Haya, 91073 Xalapa, Veracruz,México., Jiménez-Vargas JM; Facultad de Ciencias Químicas, Universidad de Colima, 28400 Coquimatlan, Colima, México., Rodríguez-Vázquez A; Centro de Conservación de Vida Silvestre El Palapo, Parcela No. 75 Z-1 P2/2, Predio Las Cuevas del Ejido Agua Zarca, 28400 Coquimatlan, Colima, México., González-Carrillo G; Tecnológico Nacional de México/ITJMMPyH, U.A. Tamazula. Carretera Tamazula Santa Rosa No. 329, 49650 Tamazula de Gordiano, Jalisco, México., Bojórquez-Velázquez E; Instituto de Ecología, Carretera antigua a Coatepec 351, El Haya, 91073 Xalapa, Veracruz,México., García-Villalvazo PE; Facultad de Ciencias Químicas, Universidad de Colima, 28400 Coquimatlan, Colima, México., Bermúdez-Guzmán MJ; Instituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias (INIFAP), 28100 Tecomán, Colima, México., Zatarain-Palacios R; Facultad de Ciencias Químicas, Universidad de Colima, 28400 Coquimatlan, Colima, México., Vázquez-Vuelvas OF; Facultad de Ciencias Químicas, Universidad de Colima, 28400 Coquimatlan, Colima, México., Valdez-Velázquez LL; Facultad de Ciencias Químicas, Universidad de Colima, 28400 Coquimatlan, Colima, México., Corzo G; Instituto de Biotecnología, Universidad Nacional Autónoma de México, 62210 Cuernavaca, Morelos, México. |
| Abstrakt: |
Heloderma horridum horridum , a venomous reptile native to America, has a venom with potential applications in treating type II diabetes. In this work, H. h. horridum venom was extracted, lyophilized, and characterized using enzymatic assays for hyaluronidase, phospholipase, and protease. Proteomic analysis of the venom was conducted employing bottom-up/shotgun approaches, SDS-PAGE, high-pH reversed-phase chromatography, and fractionation of tryptic peptides using nano-LC-MS/MS. The proteins found in H. h. horridum venom were reviewed according to the classification of the transcriptome previously reported. The proteomic approach identified 101 enzymes, 36 other proteins, 15 protein inhibitors, 11 host defense proteins, and 1 toxin, including novel venom components such as calcium-binding proteins, phospholipase A2 inhibitors, serpins, cathepsin, subtilases, carboxypeptidase-like, aminopeptidases, glycoside hydrolases, thioredoxin transferases, acid ceramidase-like, enolase, multicopper oxidases, phosphoglucose isomerase (PGI), fructose-1,6-bisphosphatase class 1, pentraxin-related, peptidylglycine α-hydroxylating monooxygenase/peptidyl-hydroxyglycine α-amidating lyase, carbonic anhydrase, acetylcholinesterase, dipeptidylpeptidase, and lysozymes. These findings contribute to understanding the venomous nature of H. h. horridum and highlight its potential as a source of bioactive compounds. Data are available via PRoteomeXchange with the identifier PXD052417. |
