Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus Carlos Corrêa-Netto a, b , Inácio de L.M. Junqueira-de-Azevedo c , d, ⁎ , Débora A. Silva c , Paulo L. Ho c , d , Moema Leitão-de-Araújo e , Maria Lúcia M. Alves e , Libia Sanz f , Débora Foguel a , Russolina Benedeta Zingali a, g , Juan J. Calvete d, ⁎⁎ a Instituto de Bioquímica Médica, Programa de Biologia Estrutural and Instituto Nacional de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Brazil b Instituto Vital Brazil, Niterói, Rio de Janeiro, Brazil c Centro de Biotecnologia, Instituto Butantan, São Paulo, Brazil d Instituto Nacional de Tecnologia em Toxinologia – INCTTox, Brazil e Fundação Zoobotânica do Rio Grande do Sul, Museu de Ciências Naturais, Núcleo Regional de Ofiologia de Porto Alegre, RS, Brazil f Instituto de Biomedicina de Valencia, CSIC, Valencia, Spain g Rede Proteômica do Rio de Janeiro, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil ARTICLE INFO ABSTRACT Available online 12 April 2011 The venom proteomes of Micrurus altirostris and M. corallinus were analyzed by combining snake venomics and venom gland transcriptomic surveys. In both coral snake species, 3FTx and PLA 2 were the most abundant and diversified toxin families. 33 different 3FTxs and 13 PLA 2 proteins, accounting respectively for 79.5% and 13.7% of the total proteins, were identified in the venom of M. altirostris. The venom of M. corallinus comprised 10 3FTx (81.7% of the venom proteome) and 4 (11.9%) PLA 2 molecules. Transcriptomic data provided the full-length amino acid sequences of 18 (M. altirostris) and 10 (M. corallinus) 3FTxs, and 3 (M. altirostris) and 1 (M. corallinus) novel PLA 2 sequences. In addition, venom from each species contained single members of minor toxin families: 3 common (PIII-SVMP, C-type lectin-like, L-amino acid oxidase) and 4 species-specific (CRISP, Kunitz-type inhibitor, lysosomal acid lipase in M. altirostris; serine proteinase in M. corallinus) toxin classes. The finding of a lipase (LIPA) in the venom proteome and in the venom gland transcriptome of M. altirostris supports the view of a recruitment event predating the divergence of Elapidae and Viperidae more than 60 Mya. The toxin profile of both M. altirostris and M. corallinus venoms points to 3FTxs and PLA 2 molecules as the major players of the envenoming process. In M. altirostris venom, all major, and most minor, 3FTxs display highest similarity to type I α-neurotoxins, suggesting that these postsynaptically acting toxins may play the predominant role in the neurotoxic effect leading to peripheral paralysis, respiratory arrest, and death. M. corallinus venom posesses both, type I α-neurotoxins and a high-abundance (26% of the venom proteome) protein of subfamily XIX of 3FTxs, exhibiting similarity to bucandin from Malayan krait, Bungarus candidus, venom, which enhances acetylcholine release presynaptically. This finding may explain the presynaptic neurotoxicity of M. corallinus venom and the lack of this effect in M. altirostris venom. The anti-Micrurus (corallinus and Keywords: Coral snake Micrurus altirostris Micrurus corallinus Snake venom proteomics Venomics Venom gland transcriptome N-terminal sequence Mass spectrometry JOURNAL OF PROTEOMICS 74 (2011) 1795 – 1809 ⁎ Correspondence to: I.L.M. Junqueira-de Azevedo, Centro de Biotecnologia, Instituto Butantan, Av. Vital Brasil 1500, 05503–900, São Paulo, Brazil. ⁎⁎ Correspondence to: J.J. Calvete, Instituto de Biomedicina de Valencia, C.S.I.C., Jaime Roig 11, 46010 Valencia, Spain. Tel.: + 34 96 339 1778; fax: +34 96 369 0800. E-mail addresses: ijuncaze@butantan.gov.br (I.L.M. Junqueira-de-Azevedo), jcalvete@ibv.csic.es (J.J. Calvete). 1874-3919/$ – see front matter © 2011 Elsevier B.V. All rights reserved. doi:10.1016/j.jprot.2011.04.003 available at www.sciencedirect.com www.elsevier.com/locate/jprot