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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Identification of hyaluronidase and phospholipase B in Lachesis muta rhombeata venom

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Autor(es):
Wiezel, Gisele A. [1] ; dos Santos, Patty K. [2] ; Cordeiro, Francielle A. [1] ; Bordon, Karla C. F. [1] ; Selistre-de-Araujo, Heloisa S. [2] ; Ueberheide, Beatrix [3] ; Arantes, Eliane C. [1]
Número total de Autores: 7
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Dept Chem & Phys, Sch Pharmaceut Sci Ribeirao Preto, BR-14040903 Ribeirao Preto, SP - Brazil
[2] Univ Fed Sao Carlos, Dept Physiol Sci, BR-13565905 Sao Carlos, SP - Brazil
[3] NYU, Langone Med Ctr, Prote Resource Ctr, New York, NY 10016 - USA
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: Toxicon; v. 107, n. B, SI, p. 359-368, DEC 1 2015.
Citações Web of Science: 11
Resumo

Hyaluronidases contribute to local and systemic damages after envenoming, since they act as spreading factors cleaving the hyaluronan presents in the connective tissues of the victim, facilitating the diffusion of venom components. Although hyaluronidases are ubiquitous in snake venoms, they still have not been detected in transcriptomic analysis of the Lachesis venom gland and neither in the proteome of its venom performed previously. This work purified a hyaluronidase from Lachesis mum rhombeata venom whose molecular mass was estimated by SDS-PAGE to be 60 kDa. The hyaluronidase was more active at pH 6 and 37 degrees C when salt concentration was kept constant and more active in the presence of 0.15 M monovalent ions when the pH was kept at 6. Venom was fractionated by reversed-phase liquid chromatography (RPLC). Edman sequencing after RPLC failed to detect hyaluronidase, but identified a new serine proteinase isoform. The hyaluronidase was identified by mass spectrometry analysis of the protein bands in SDS-PAGE. Additionally, phospholipase B was identified for the first time in Lachesis genus venom. The discovery of new bioactive molecules might contribute to the design of novel drugs and biotechnology products as well as to development of more effective treatments against the envenoming. (C) 2015 Elsevier Ltd. All rights reserved. (AU)

Processo FAPESP: 11/23236-4 - Toxinas animais nativas e recombinantes: análise funcional, estrutural e molecular
Beneficiário:Suely Vilela
Linha de fomento: Auxílio à Pesquisa - Temático
Processo FAPESP: 10/06199-5 - "purificação e caracterização bioquímica da hialuronidase presente na peçonha de Lachesis muta"
Beneficiário:Gisele Adriano Wiezel
Linha de fomento: Bolsas no Brasil - Iniciação Científica