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Título : | Characterization of toxins from the broad-banded water snake Helicops angulatus (Linnaeus, 1758): isolation of a cysteine-rich secretory protein, Helicopsin |
Autor : | Estrella, Amalid Sánchez, Elda E Galán, Jacob A Tao, W. Andy ·Guerrero, Belsy Navarrete, Luis F Rodríguez-Acosta, Alexis |
Palabras clave : | CRISP Colubroidea Dipsadidae salivary excretion Neurotoxin Helicops angulatus |
Fecha de publicación : | 27-Nov-2013 |
Citación : | Archives of Toxicology;85(4):305-13. 2011 |
Resumen : | Helicops angulatus (broad-banded water snake)
according to recent proposals is presently cited in the family
Dipsadidae, subfamily Xenodontinae, forming the tribe
Hydropsini along with the genera Hydrops and Pseudoeryx.
The current work characterizes the proteolytic and neurotoxic
activities of H. angulatus crude toxins from salivary
excretion (SE) and describes the isolation and identiWcation
of a cysteine-rich secretory protein (CRISP) called helicopsin.
The SE lethal dose (LD50) was 5.3 mg/kg; however, the
SE did not contain hemorrhagic activity. Helicopsin was
puriWed using activity-guided, Superose 12 10/300 GL
molecular exclusion, Mono Q10 ion exchange, and Protein
Pak 60 molecular exclusion. Sodium dodecyl sulfate–polyacrylamide
gel electrophoresis (SDS–PAGE) showed a
highly puriWed band of approximately 20 kDa. The minimal
lethal dose for helicopsin was 0.4 mg/kg. Liquid chromatography
mass spectrometry (LC-MS/MS) analysis
identiWed 2 unique peptides MEWYPEAAANAER and
YTQIVWYK, representing a protein sequence (deleted
homology) belonging to cysteine-rich secretory proteins,
which are conserved in snake venoms (CRISPs). CRISPs
are a large family of cysteine-rich secretory proteins found
in various organisms and participate in diverse biological
processes. Helicopsin exhibited robust neurotoxic activity
as evidenced by immediate death (»8 min) due to respiratory
paralysis in NIH mice. These observations for helicopsin
puriWed from H. angulatus provide further evidence of
the extensive distribution of highly potent neurotoxins in
the Colubroidea superfamily of snakes than previously
described. |
URI : | http://hdl.handle.net/10872/5112 |
Aparece en las colecciones: | Artículos Publicados
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