Identification and partial characterisation of hyaluronidases in Lonomia obliqua venom

Identification and partial characterisation of hyaluronidases in Lonomia obliqua venom

Author Gouveia, AID Google Scholar
Silveira, R. B. da Google Scholar
Nader, H. B. Google Scholar
Dietrich, C. P. Google Scholar
Gremski, W. Google Scholar
Veiga, S. S. Google Scholar
Institution Univ Fed Parana
Universidade Federal de São Paulo (UNIFESP)
Catholic Univ Parana
Abstract By studying Lonomia obliqua (caterpillar) venom we were able to detect a lytic activity on purified hyaluronic acid. the venom hydrolyses purified chondroitin sulphate, but was unable to degrade either heparan sulphate or dermatan sulphate. Moreover, through purified hyaluronic acid-degrading kinetic assays, we observed that this lytic activity was caused by a hydrolase rather than lyase enzyme. in addition, by using the Reissig colorimetric reaction, we detected this hyaluronic acid hydrolase action as a beta-endohexosaminidase enzyme originating terminal N-acetylglucosamine residues rather than beta-endoglucuronidase, which may originate glucuronic acid residues. Zymogram analysis of the venom detected 49 and 53 kDa molecules with hyaluronic acid lyric activity. An examination of these hyaluronic acid degrading activities as a function of pH showed that these hydrolases had no apparent activities at a pH below 5.0 and higher than 8.0 and displayed their optimal activities at pH ranging from 6.0 to 7.0. Finally, through a fluorescence reaction to hyaluronic acid and confocal microscopy, we confirmed this cleaving action upon hyaluronic acid organised on the extracellular matrix of the dermis of rabbit. the data provide experimental evidence of the presence of hyaluronidases in the L. obliqua venom, probably involved in the harmful effects of the venom. (c) 2004 Published by Elsevier B.V.
Keywords Lonomia obliqua
Language English
Date 2005-03-15
Published in Toxicon. Oxford: Pergamon-Elsevier B.V., v. 45, n. 4, p. 403-410, 2005.
ISSN 0041-0101 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 403-410
Access rights Closed access
Type Article
Web of Science ID WOS:000227580500003

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