Please use this identifier to cite or link to this item: https://doi.org/10.1021/pr901044x
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dc.titleIdentification of a novel family of snake venom proteins veficolins from cerberus rynchops using a venom gland transcriptomics and proteomics approach
dc.contributor.authorOmpraba, G.
dc.contributor.authorChapeaurouge, A.
dc.contributor.authorDoley, R.
dc.contributor.authorDevi, K.R.
dc.contributor.authorPadmanaban, P.
dc.contributor.authorVenkatraman, C.
dc.contributor.authorVelmurugan, D.
dc.contributor.authorLin, Q.
dc.contributor.authorKini, R.M.
dc.date.accessioned2014-10-27T08:30:57Z
dc.date.available2014-10-27T08:30:57Z
dc.date.issued2010-04-05
dc.identifier.citationOmpraba, 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
dc.identifier.issn15353893
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100867
dc.description.abstractCerberus 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/pr901044x
dc.sourceScopus
dc.subjectInnate immunity
dc.subjectSnake venom toxicity
dc.subjectVenom proteome
dc.subjectVenom transcriptome
dc.subjectVenomics
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/pr901044x
dc.description.sourcetitleJournal of Proteome Research
dc.description.volume9
dc.description.issue4
dc.description.page1882-1893
dc.description.codenJPROB
dc.identifier.isiut000276215700024
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