Venomics Profiling of Thamnodynastes strigatus Unveils Matrix Metalloproteinases and Other Novel Proteins Recruited to the Toxin Arsenal of Rear-Fanged Snakes
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
29/10/2013
29/10/2013
2012
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Resumo |
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 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 (similar to 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. Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) Fundacao de Amparo a Pesquisa do Estado de Rio de Janeiro (FAPERJ) Fundacao de Amparo a Pesquisa do Estado do Rio de Janeiro (FAPERJ) Fundacao Oswaldo Cruz/PDTIS Fundacao Oswaldo Cruz/PDTIS Instituto Nacional de Ciencia e Tecnologia em Toxinologia (INCTTox) Instituto Nacional de Ciencia e Tecnologia em Toxinologia (INCTTox) |
Identificador |
JOURNAL OF PROTEOME RESEARCH, WASHINGTON, v. 11, n. 2, supl. 1, Part 1, pp. 1152-1162, FEB, 2012 1535-3893 http://www.producao.usp.br/handle/BDPI/36287 10.1021/pr200876c |
Idioma(s) |
eng |
Publicador |
AMER CHEMICAL SOC WASHINGTON |
Relação |
JOURNAL OF PROTEOME RESEARCH |
Direitos |
closedAccess Copyright AMER CHEMICAL SOC |
Palavras-Chave | #SNAKE #VENOM #TOXIN #TRANSCRIPTOME #PROTEOME #MATRIX METALLOPROTEINASE #GEL-ELECTROPHORESIS #GLAND TRANSCRIPTOME #DUVERNOYS GLAND #COLUBRID SNAKES #HUMAN GENE #PIT VIPER #EVOLUTION #FAMILY #EXPRESSION #SIMILARITIES #BIOCHEMICAL RESEARCH METHODS |
Tipo |
article original article publishedVersion |