Proteomic Characterization of the Hyaluronidase (EC 3.2.1.35) from the Venom of the Social Wasp Polybia paulista

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art_ARCURI_Proteomic_Characterization_of_the_Hyaluronidase_(EC_3_2_2012.PDF (404.73 KB)
Citações na Scopus
20
Tipo de produção
article
Data de publicação
2012
Editora
BENTHAM SCIENCE PUBL LTD
DOI
Indexadores
Scopus
Web of Science
PubMed
Título da Revista
ISSN da Revista
Título do Volume
Autores
PINTO, Jose Roberto Aparecido dos Santos
SANTOS, Lucilene Delazari dos
DIAS, Nathalia Baptista
PALMA, Mario Sergio
Autor de Grupo de pesquisa
Editores
Coordenadores
Organizadores
Citação
PROTEIN AND PEPTIDE LETTERS, v.19, n.6, p.625-635, 2012
Projetos de Pesquisa
Unidades Organizacionais
Fascículo
Resumo
Polybia paulista wasp venom possesses three major allergens: phospholipase A(1), hyaluronidase and antigen-5. To the best of our knowledge, no hyaluronidase from the venom of Neotropical social wasps was structurally characterized up to this moment, mainly due to its reduced amount in the venom of the tropical wasp species (about 0.5% of crude venom). Four different glycoproteic forms of this enzyme were detected in the venom of the wasp Polybia paulista. In the present investigation, an innovative experimental approach was developed combining 2-D SDS-PAGE with in-gel protein digestion by different proteolytic enzymes, followed by mass spectrometry analysis under collision-induced dissociation CID) conditions for the complete assignment of the protein sequencing. Thus, the most abundant form of this enzyme in P. paulista venom, the hyaluronidase-III, was sequenced, revealing that the first 47 amino acid residues from the N-terminal region, common to other Hymenoptera venom hyaluronidases, are missing. The molecular modeling revealed that hyaluronidase-III has a single polypeptide chain, folded into a tertiary structure, presenting a central (beta/alpha)(5) core with alternation of beta-strands and alpha-helices; the tertiary structure stabilized by a single disulfide bridge between the residues Cys(189) and Cys(201). The structural pattern reported for P. paulista venom hyaluronidase-III is compatible with the classification of the enzyme as member of the family 56 of glycosidase hydrolases. Moreover, its structural characterization will encourage the use of this protein as a model for future development of ""component-resolved diagnosis"".
Palavras-chave
Allergen, hyaluronidase, mass spectrometry, molecular modeling, peptide sequencing, wasp venom
URI
https://observatorio.fm.usp.br/handle/OPI/4336
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Coleções
Artigos e Materiais de Revistas Científicas - FM/Outros