3 research outputs found
Individual Variability in the Venom Proteome of Juvenile <i>Bothrops jararaca</i> Specimens
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.
LCāMS 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
Venomics Profiling of <i>Thamnodynastes strigatus</i> Unveils Matrix Metalloproteinases and Other Novel Proteins Recruited to the Toxin Arsenal of Rear-Fanged Snakes
Rear-fanged and aglyphous snakes are usually considered
not dangerous
to humans because of their limited capacity of injecting venom. Therefore,
only a few studies have been dedicated to characterizing the venom
of the largest parcel of snake fauna. Here, we investigated the venom
proteome of the rear-fanged snake <i>Thamnodynastes
strigatus</i>, in combination with a transcriptomic
evaluation of the venom gland. About 60% of all transcripts code for
putative venom components. A striking finding is that the most abundant
type of transcript (ā¼47%) and also the major protein type in
the venom correspond to a new kind of matrix metalloproteinase (MMP)
that is unrelated to the classical snake venom metalloproteinases
found in all snake families. These enzymes were recently suggested
as possible venom components, and we show here that they are proteolytically
active and probably recruited to venom from a MMP-9 ancestor. Other
unusual proteins were suggested to be venom components: a protein
related to lactadherin and an EGF repeat-containing transcript. Despite
these unusual molecules, seven toxin classes commonly found in typical
venomous snakes are also present in the venom. These results support
the evidence that the arsenals of these snakes are very diverse and
harbor new types of biologically important molecules
Venomics Profiling of <i>Thamnodynastes strigatus</i> Unveils Matrix Metalloproteinases and Other Novel Proteins Recruited to the Toxin Arsenal of Rear-Fanged Snakes
Rear-fanged and aglyphous snakes are usually considered
not dangerous
to humans because of their limited capacity of injecting venom. Therefore,
only a few studies have been dedicated to characterizing the venom
of the largest parcel of snake fauna. Here, we investigated the venom
proteome of the rear-fanged snake <i>Thamnodynastes
strigatus</i>, in combination with a transcriptomic
evaluation of the venom gland. About 60% of all transcripts code for
putative venom components. A striking finding is that the most abundant
type of transcript (ā¼47%) and also the major protein type in
the venom correspond to a new kind of matrix metalloproteinase (MMP)
that is unrelated to the classical snake venom metalloproteinases
found in all snake families. These enzymes were recently suggested
as possible venom components, and we show here that they are proteolytically
active and probably recruited to venom from a MMP-9 ancestor. Other
unusual proteins were suggested to be venom components: a protein
related to lactadherin and an EGF repeat-containing transcript. Despite
these unusual molecules, seven toxin classes commonly found in typical
venomous snakes are also present in the venom. These results support
the evidence that the arsenals of these snakes are very diverse and
harbor new types of biologically important molecules