Proteomic Analysis of Heloderma horridum horridum Venom: Assessment to Its Transcriptome and Newfound Proteins


Por: Lino-López, GJ, Ruiz-May, E, Elizalde-Contreras, JM, Jiménez-Vargas, JM, Rodríguez-Vázquez, A, González-Carrillo, G, Bojórquez-Velázquez, E, García-Villalvazo, PE, Bermúdez-Guzmán, MD, Zatarain-Palacios, R, Vázquez-Vuelvas, OF, Valdez-Velázquez, LL, Corzo, G

Publicada: 22 jul 2024 Ahead of Print: 1 jul 2024
Resumen:
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 alpha-hydroxylating monooxygenase/peptidyl-hydroxyglycine alpha-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.

Filiaciones:
Lino-López, GJ:
 Univ Colima, Fac Ciencias Quim, Colima 28400, Mexico

 CNRF DGSV SENAS SADER, Dept Control Biol, Colima 28110, Mexico

Ruiz-May, E:
 Inst Ecol, Xalapa 91073, Veracruz, Mexico

Elizalde-Contreras, JM:
 Inst Ecol, Xalapa 91073, Veracruz, Mexico

Jiménez-Vargas, JM:
 Univ Colima, Fac Ciencias Quim, Colima 28400, Mexico

Rodríguez-Vázquez, A:
 Ctr Conservac Vida Silvestre El Palapo, Colima 28400, Mexico

González-Carrillo, G:
 Tecnol Nacl Mexico ITJMMPyH, UA Tamazula, Tamazula De Gordiano 49650, Jalisco, Mexico

Bojórquez-Velázquez, E:
 Inst Ecol, Xalapa 91073, Veracruz, Mexico

García-Villalvazo, PE:
 Univ Colima, Fac Ciencias Quim, Colima 28400, Mexico

Bermúdez-Guzmán, MD:
 INIFAP, Colima 28100, Mexico

Zatarain-Palacios, R:
 Univ Colima, Fac Ciencias Quim, Colima 28400, Mexico

Vázquez-Vuelvas, OF:
 Univ Colima, Fac Ciencias Quim, Colima 28400, Mexico

Valdez-Velázquez, LL:
 Univ Colima, Fac Ciencias Quim, Colima 28400, Mexico

Corzo, G:
 Univ Nacl Autonoma Mexico, Inst Biotecnol, Cuernavaca 62210, Morelos, Mexico
ISSN: 15353893
Editorial
American Chemical Society, 1155 16TH ST, NW, WASHINGTON, DC 20036 USA, Estados Unidos America
Tipo de documento: Article
Volumen: 23 Número: 8
Páginas: 3638-3648
WOS Id: 001274514000001
ID de PubMed: 39038168

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