Citation

Batista CVF, Martins JG, Restano-Cassulini R, Coronas FIV, Zamudio FZ, Procópio R, Possani LD. Toxicon 2018; 143: 51-58.

Affiliation

Departmento de Medicina Molecular y Bioprocesos, Instituto de Biotecnologia, Universidad Nacional Autónoma de México, Avenida Universidad, 2001, Cuernavaca, Morelos 62210, Mexico. Electronic address: possani@ibt.unam.mx.

Copyright

(Copyright © 2018, Elsevier Publishing)

DOI

10.1016/j.toxicon.2018.01.006

PMID

29337221

Abstract

The soluble venom from the scorpion Tityus metuendus was characterized by various methods. In vivo experiments with mice showed that it is lethal. Extended electrophysiological recordings using seven sub-types of human voltage gated sodium channels (hNav1.1 to 1.7) showed that it contains both α- and β-scorpion toxin types. Fingerprint analysis by mass spectrometry identified over 200 distinct molecular mass components. At least 60 sub-fractions were recovered from HPLC separation. Five purified peptides were sequenced by Edman degradation, and their complete primary structures were determined. Additionally, three other peptides have had their N-terminal amino acid sequences determined by Edman degradation and reported. Mass spectrometry analysis of tryptic digestion of the soluble venom permitted the identification of the amino acid sequence of 111 different peptides. Search for similarities of the sequences found indicated that they probably are: sodium and potassium channel toxins, metalloproteinases, hyaluronidases, endothelin and angiotensin-converting enzymes, bradykinin-potentiating peptide, hypothetical proteins, allergens, other enzymes, other proteins and peptides.

Copyright © 2018. Published by Elsevier Ltd.

Language: en

Keywords

Amino acid sequence; Na(+)-channel; Proteome analysis; Scorpion venom; Tityus metuendus