Please use this identifier to cite or link to this item: https://doi.org/10.1021/pr901044x
Title: Identification of a novel family of snake venom proteins veficolins from cerberus rynchops using a venom gland transcriptomics and proteomics approach
Authors: Ompraba, G.
Chapeaurouge, A.
Doley, R. 
Devi, K.R.
Padmanaban, P.
Venkatraman, C.
Velmurugan, D.
Lin, Q. 
Kini, R.M. 
Keywords: Innate immunity
Snake venom toxicity
Venom proteome
Venom transcriptome
Venomics
Issue Date: 5-Apr-2010
Citation: Ompraba, G., Chapeaurouge, A., Doley, R., Devi, K.R., Padmanaban, P., Venkatraman, C., Velmurugan, D., Lin, Q., Kini, R.M. (2010-04-05). Identification of a novel family of snake venom proteins veficolins from cerberus rynchops using a venom gland transcriptomics and proteomics approach. Journal of Proteome Research 9 (4) : 1882-1893. ScholarBank@NUS Repository. https://doi.org/10.1021/pr901044x
Abstract: Cerberus rynchops (dog-faced water snake) belongs to Homalopsidae of Colubroidea (rear-fanged snakes). So far, venom compositions of snakes of the Homalopsidae family are not known. To determine the venom composition of C. rynchops, we have used both transcriptomics and proteomics approaches. The venom gland transcriptome revealed 104 ESTs and the presence of three known snake protein families, namely, metalloprotease, CRISP, and C-type lectin. In addition, we identified two proteins that showed sequence homology to ficolin, a mammalian protein with collagen-like and fibrinogen-like domains. We named them as ryncolin 1 and ryncolin 2 (rynchops ficolin) and this new family of snake venom proteins as veficolins (venom ficolins). On the basis of its structural similarity to ficolin, we speculate that ryncolins may induce platelet aggregation and/or initiate complement activation. To determine the proteome, the whole C. rynchops venom was trypsinized and fractionated by reverse phase HPLC followed by MALDI-MS/MS analysis of the tryptic peptides. Analysis of the tandem mass spectrometric data indicated the presence of all protein families compared to the translated cDNA library. Overall, our combined approach of transcriptomics and proteomics revealed that C. rynchops venom is among the least complex snake venom characterized to date despite the presence of a new family of snake venom proteins. © 2010 American Chemical Society.
Source Title: Journal of Proteome Research
URI: http://scholarbank.nus.edu.sg/handle/10635/100867
ISSN: 15353893
DOI: 10.1021/pr901044x
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