Proteomics of the neurotoxic fraction from the sea anemone Bunodosoma cangicum venom: Novel peptides belonging to new classes of toxins

Autor(es)

Zaharenko, Andre Junqueira ^[1] ; Ferreira, Jr., Wilson Alves ^[1] ; Oliveira, Joacir Stolarz ^[1] ; Richardson, Michael ^[2] ; Pimenta, Daniel Carvalho ^[3] ; Konno, Katsuhiro ^[4] ; Portaro, Fernanda C. V. ^[5] ; de Freitas, Jose Carlos ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Dept Fisiol, Inst Biociencias, BR-05508900 Sao Paulo - Brazil

^[2] Fdn Ezequiel Dias FUNED, BR-30510010 Belo Horizonte, MG - Brazil

^[3] Inst Butantan, Lab Bioquim & Biofis, BR-05503900 Sao Paulo - Brazil

^[4] Toyama Univ, Inst Nat Med, Toyama 9300194 - Japan

^[5] Inst Butantan, Lab Imunoquim, BR-05503900 Sao Paulo - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Comparative Biochemistry and Physiology D-Genomics & Proteomics; v. 3, n. 3, p. 219-225, SEP 2008.
• Citações Web of Science: 29

Resumo

In contrast to the many studies on the venoms of scorpions, spiders, snakes and cone snails, tip to now there has been no report of the proteomic analysis of sea anemones venoms. In this work we report for the first time the peptide mass fingerprint and some novel peptides in the neurotoxic fraction (Fr III) of the sea anemone Bunodosoma cangicum venom. Fr III is neurotoxic to crabs and was purified by rp-HPLC in a C-18 column, yielding 41 fractions. By checking their molecular masses by ESI-Q-Tof and MALDI-Tof MS we found 81 components ranging from near 250 amu to approximately 6000 amu. Some of the peptidic molecules were partially sequenced through the automated Edman technique. Three of them are peptides with near 4500 amu belonging to the class of the BcIV, BDS-I, BDS-II, APETx1, APETx2 and Am-II toxins. Another three peptides represent a novel group of toxins (similar to 3200 amu). A further three molecules (similar to similar to 4900 amu) belong to the group of type 1 sodium channel neurotoxins. When assayed over the crab leg nerve compound action potentials, one of the BcIV- and APETx-like peptides exhibits an action similar to the type 1 sodium channel toxins in this preparation, suggesting the same target in this assay. On the other hand one of the novel peptides, with 3176 amu, displayed an action similar to potassium channel blockage in this experiment. In summary, the proteomic analysis and mass fingerprint of fractions from sea anemone venoms through MS are valuable tools, allowing us to rapidly predict the occurrence of different groups of toxins and facilitating the search and characterization of novel molecules without the need of full characterization of individual components by broader assays and bioassay-guided purifications. It also shows that sea anemones employ dozens of components for prey capture and defense. (C) 2008 Elsevier Inc. All rights reserved. (AU)

• Processo FAPESP: 01/14243-5 - Investigação de peptídeos dos nematocistos da anêmona do mar Bunodosoma cangicum (Cnidaria, Anthozoa, Actiniidae)
• Beneficiário: Andre Junqueira Zaharenko
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto