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

Author(s)

Aparecido dos Santos Pinto, Jose Roberto ^{[1, 2]} ; dos Santos, Lucilene Delazari ^{[1, 2]} ; Arcuri, Helen Andrade ^{[2, 3]} ; Dias, Nathalia Baptista ^{[1, 2]} ; Palma, Mario Sergio ^{[1, 2]}

Affiliation

^[1] UNESP Univ Estadual Paulista, Sao Paulo State Univ, Inst Biosci Rio Claro, Ctr Study Social Insects, Dept Biol, Rio Claro, SP - Brazil

^[2] Inst Res Immunol INCT Iii, Sao Paulo - Brazil

^[3] INCOR HC FMUSP, Discipline Allergy & Immunol, Sao Paulo - Brazil

• Document type: Journal article
• Source: PROTEIN AND PEPTIDE LETTERS; v. 19, n. 6, p. 625-635, JUN 2012.
• Web of Science Citations: 15

Abstract

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{''}. (AU)

• FAPESP's process: 11/51684-1 - System biology as experimental strategy for discovery of novel natural products in the fauna of venomous arthropods from São Paulo State
• Grantee: Mario Sergio Palma
• Support Opportunities: BIOTA-FAPESP Program - Thematic Grants