| dc.description.abstract | Venoms of the redtail coral snake Micrurus mipartitus from Colombia and Costa Rica were
analyzed by “venomics”, a proteomic strategy to determine their composition. Proteins
were separated by RP-HPLC, followed by SDS-PAGE, in-gel tryptic digestion, identification
by MALDI or ESI tandem mass spectrometry, and assignment to known protein families
by similarity. These analyses were complemented with a characterization of venom activities
in vitro and in vivo. Proteins belonging to seven families were found in Colombian M.
mipartitus venom, including abundant three-finger toxins (3FTx; ~60% of total proteins)
and phospholipases A2 (PLA2; ~30%), with the remaining ~10% distributed among L-amino
acid oxidase, P-III metalloproteinase, Kunitz-type inhibitor, serine proteinase, and C-type
lectin-like families. The venoms of two M. mipartitus specimens from Costa Rica, also referred
to as M. multifasciatus in some taxonomic classifications, were also analyzed. Both
samples were highly similar to each other, and partially resembled the chromatographic
and identity profiles of M. mipartitus from Colombia, although presenting a markedly higher
proportion of 3FTxs (~83.0%) in relation to PLA2s (~8.2%), and a small amount of acetylcholinesterase,
not detected in the venom from Colombia. An equine antivenom against the
Central American coral snake, M. nigrocinctus, did not recognize venom components of M.
mipartitus from Colombia or Costa Rica by enzyme-immunoassay. Four major components
of Colombian M. mipartitus venom were isolated and partially characterized. Venomics of
Micrurus species may provide a valuable platform for the rational design of immunizing
cocktails to obtain polyspecific antivenoms for this highly diverse group of American
elapids. | |
