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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Identification of hyaluronidase and phospholipase B in Lachesis muta rhombeata venom

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Author(s):
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]
Total Authors: 7
Affiliation:
[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
Total Affiliations: 3
Document type: Journal article
Source: Toxicon; v. 107, n. B, SI, p. 359-368, DEC 1 2015.
Web of Science Citations: 11
Abstract

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)

FAPESP's process: 11/23236-4 - Native and recombinant animal toxins: functional, structural and molecular analysis
Grantee:Suely Vilela
Support type: Research Projects - Thematic Grants
FAPESP's process: 10/06199-5 - "purification and biochemical characterization of hyaluronidase present in the venom of Lachesis muta "
Grantee:Gisele Adriano Wiezel
Support type: Scholarships in Brazil - Scientific Initiation