2 research outputs found
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 (∼47%) 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 (∼47%) 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