Proteomic analysis of the venom from the scorpion Tityus stigmurus: biochemical and physiological comparison with other Tityus species.
The venom from the Brazilian scorpion Tityus stigmurus was fractionated by high performance liquid chromatography (HPLC) and the corresponding components were used for molecular mass determination using electrospray ion trap mass spectrometry. One hundred distinct components were clearly assigned showing molecular masses from 216.5 to 44,800.0 Da. Fifteen new components were isolated and sequenced, four of them to completion: Tst-3 (similar to Na(+) channel specific scorpion toxins), Tst-17 (a K(+) channel blocking peptide similar to Tc1), Tst beta KTx (a peptide with identical sequence as that of TsTX-K beta toxin earlier described to exist in T. serrulatus venom) and finally a novel proline-rich peptide of unknown function. Among the eleven components partially sequenced were two enzymes: hyaluronidase and lysozyme. The first enzyme has a molecular mass of 44,800.0 Da. This enzyme showed high activity against the substrate hyaluronan in vitro. Amino acid sequence of the second enzyme showed that it is similar to other known lysozymes, with similar molecular mass and sequence to that of bona fide lysozymes reported in public protein data banks. Finally, this communication reports a correlation among HPLC retention times and molecular masses of folded scorpion toxins as well as a comparative structural and physiological analysis of components from the venom of several species of the genus Tityus.
Batista
C V F
CVF
Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico, Avenida Universidad, 2001, Apartado Postal 510-3, Cuernavaca 62210, Mexico.
Román-González
S A
SA
Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico, Avenida Universidad, 2001, Apartado Postal 510-3, Cuernavaca 62210, Mexico.
Salas-Castillo
S P
SP
Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico, Avenida Universidad, 2001, Apartado Postal 510-3, Cuernavaca 62210, Mexico.
Zamudio
F Z
FZ
Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico, Avenida Universidad, 2001, Apartado Postal 510-3, Cuernavaca 62210, Mexico.
Gómez-Lagunas
F
F
Department of Physiology, Medical School, National Autonomous University of Mexico, Ciudad Universitaria, Mexico D.F. 04510, Mexico.
Possani
L D
LD
Department of Molecular Medicine and Bioprocesses, Institute of Biotechnology, National Autonomous University of Mexico, Avenida Universidad, 2001, Apartado Postal 510-3, Cuernavaca 62210, Mexico. Electronic address: possani@ibt.unam.mx.
D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D002851:Chromatography, High Pressure Liquid; D004594:Electrophysiology; D006821:Hyaluronoglucosaminidase / Q000032:analysis; D019476:Insect Proteins / Q000737:chemistry* / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009113:Muramidase / Q000032:analysis; D018408:Patch-Clamp Techniques; D010449:Peptide Mapping; D026902:Potassium Channel Blockers / Q000737:chemistry* / Q000494:pharmacology; D040901:Proteomics; D012604:Scorpion Venoms / Q000737:chemistry* / Q000494:pharmacology; D012605:Scorpions; D051637:Shaker Superfamily of Potassium Channels / Q000187:drug effects / Q000378:metabolism; D013045:Species Specificity; D021241:Spectrometry, Mass, Electrospray Ionization; D018411:Spodoptera / Q000166:cytology / Q000187:drug effects
D019476:Insect Proteins; D026902:Potassium Channel Blockers; D012604:Scorpion Venoms; D051637:Shaker Superfamily of Potassium Channels; D009113:Muramidase; D006821:Hyaluronoglucosaminidase