Citation

Ching AT, Paes Leme AF, Zelanis A, Rocha MM, Furtado MD, Silva DA, Trugilho MR, Rocha SL, Perales J, Ho PL, Serrano SM, Junqueira-de-Azevedo IL. J. Proteome Res. 2011; 11(2): 1152-1162.

Copyright

(Copyright © 2011, American Chemical Society)

DOI

10.1021/pr200876c

PMID

22168127

Abstract

Rear-fanged and aglyphous snakes are usually considered not dangerous to humans due to their limited capacity of injecting venom. Therefore, only few studies have been dedicated to characterize the venom of the largest parcel of snake fauna. Here, we investigated the venom proteome of the rear-fanged snake Thamnodynastes strigatus, 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 (SVMPs) found in all snake families. These enzymes were recently suggested as possible venom components and we shown 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. These results support the evidences that the arsenals of these snakes are very diverse and harbor new types of biologically important molecules.

Language: en