title: Characterising the enzymatic profile of crude tentacle extracts from the South Atlantic jellyfish Olindias sambaquiensis (Cnidaria: Hydrozoa).
abstract: Jellyfish venoms are of medical and biotechnological importance, with toxins displaying antimicrobial, analgesic and anti-tumor activities. Although proteolytic enzymes have also been described, detailed characterisation of these proteins is scant in Olindias spp. High throughput mass spectrometry profiling of cnidarian venoms has become increasingly popular since the first description of the proteomic profile of putative toxins isolated from nematocysts of the hydrozoan jellyfish Olindias sambaquiensis describing the presence of orthologous enzymes as presented in venoms of advanced species as snakes. Rigorous bioinformatics analyses can aid functional annotation, but biochemical assays are prerequisite to unambiguously assign toxic function to a peptide or protein. Here we present results that experimentally confirm previously predicted proteomic analysis that crude venom extracts from tentacles of O. sambaquiensis are composed of polypeptides with metalloproteinase, serine proteinase and phospholipases A2 activities. Surprisingly, levels of serine proteinase and phospholipase A2 activities were comparable to those observed in venoms of Bothrops snakes which were used as positive controls in this study. Hence, these data offer new opportunities to explore serine proteinase and phospholipase A2 activities in the clinical sequelae following O. sambaquiensis envenomation, with future possible biopharmaceutical applications.
authors.affiliation: Laboratório de Imunopatologia, Instituto Butantan, Av. Vital Brasil 1500, 05503-900 São Paulo, SP, Brazil.
authors.forename: Paloma S
authors.initials: PS
authors.lastname: Knittel
authors.affiliation: Institute of Pharmaceutical Science, King's College London, United Kingdom; Department of Chemistry, King's College London, United Kingdom; Brazil Institute, King's College London, United Kingdom; Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Av. Prof. Lineu Prestes, 580, B16, 05508-000 São Paulo, SP, Brazil.
authors.forename: Paul F
authors.initials: PF
authors.lastname: Long
authors.affiliation: Institute of Pharmaceutical Science, King's College London, United Kingdom.
authors.forename: Lucas
authors.initials: L
authors.lastname: Brammall
authors.affiliation: Departamento de Zoologia, Instituto de Biociências, Universidade de São Paulo, Rua do Matao, Trav. 14, 101, 05508-090 São Paulo, SP, Brazil; Centro de Biologia Marinha, Universidade de São Paulo, Rodovia Manoel Hypólito do Rego, km. 131, 11600-000 São Sebastião, Brazil.
authors.forename: Antonio C
authors.initials: AC
authors.lastname: Marques
authors.affiliation: Laboratório de Imunopatologia, Instituto Butantan, Av. Vital Brasil 1500, 05503-900 São Paulo, SP, Brazil.
authors.forename: Michelle T
authors.initials: MT
authors.lastname: Almeida
authors.affiliation: Instituto de Ciências Biomédicas, Universidade de São Paulo, Av. Prof. Lineu Prestes, 2415, 05508-900 São Paulo, SP, Brazil.
authors.forename: Gabriel
authors.initials: G
authors.lastname: Padilla
authors.affiliation: Laboratório de Imunopatologia, Instituto Butantan, Av. Vital Brasil 1500, 05503-900 São Paulo, SP, Brazil. Electronic address: ana.moura@butantan.gov.br.
authors.forename: Ana M
authors.initials: AM
authors.lastname: Moura-da-Silva
mesh_terms: D000818:Animals; D003064:Cnidarian Venoms / Q000737:chemistry* / Q000201:enzymology; D045726:Metalloproteases / Q000378:metabolism; D054467:Phospholipases A2 / Q000378:metabolism; D059748:Proteolysis; D057057:Serine Proteases / Q000378:metabolism
chemical_list: D003064:Cnidarian Venoms; D054467:Phospholipases A2; D045726:Metalloproteases; D057057:Serine Proteases
keywords: Cnidaria; Metalloproteinase; Olindias sambaquiensis; Phospholipase A(2); Serine proteinase; Venom