Individual Variability in the Venom Proteome of Juvenile <i>Bothrops jararaca</i> Specimens
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Abstract
Snake venom proteomes/peptidomes
are highly complex and subject
to ontogenetic changes. Individual variation in the venom proteome
of juvenile snakes is poorly known. We report the proteomic analysis
of venoms from 21 juvenile specimens of <i>Bothrops jararaca</i> of different geographical origins and correlate it with the evaluation
of important venom features. Individual venoms showed similar caseinolytic
activities; however, their amidolytic activities were significantly
different. Rather intriguingly, plasma coagulant activity showed remarkable
variability among the venoms but not the prothrombin-activating activity.
LC–MS analysis showed significant differences between venoms;
however, an interesting finding was the ubiquitous presence of the
tripeptide ZKW, an endogenous inhibitor of metalloproteinases. Electrophoretic
profiles of proteins submitted to reduction showed significant variability
in total proteins, glycoproteins, and in the subproteomes of proteinases.
Moreover, identification of differential bands revealed variation
in most <i>B. jararaca</i> toxin classes. Profiles of venoms
analyzed under nonreducing conditions showed less individual variability
and identification of proteins in a conserved band revealed the presence
of metalloproteinases and l-amino acid oxidase as common
components of these venoms. Taken together, our findings suggest that
individual venom proteome variability in <i>B. jararaca</i> exists from a very early animal age and is not a result of ontogenetic
and diet changes