Self-assembly and Structural Characterization of Echinococcus Granulosus Antigen B Recombinant Subunit Oligomers.
From: Laboratório de Biologia Molecular de Cestódeos, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Cx. Postal 15005, 91501-970, Porto Alegre, RS, Brazil.
Biochimica et biophysica acta
- Publish Date: Feb 2007
- ISSN: 0006-3002
- Volume: 1774
- Issue: 2
- Pages: 278-85
- Medium: Print
- Language: English
- Citation (JAMA): Monteiro Karina M, Scapin Sandra M N, Navarro Marcos V A S, et al. Self-assembly and Structural Characterization of Echinococcus Granulosus Antigen B Recombinant Subunit Oligomers.. Biochim. Biophys. Acta Feb 2007;1774:278-85
Abstract
Echinococcus granulosus antigen B is an oligomeric protein of 120-160 kDa composed by 8-kDa (AgB8) subunits. Here, we demonstrated that the AgB8 recombinant subunits AgB8/1, AgB8/2 and AgB8/3 are able to self-associate into high order homo-oligomers, showing similar properties to that of parasite-produced AgB, making them valuable tools to study AgB structure. Dynamic light scattering, size exclusion chromatography and cross-linking assays revealed approximately 120- to 160-kDa recombinant oligomers, with a tendency to form populations with different aggregation states. Recombinant oligomers showed helical circular dichroism spectra and thermostability similar to those of purified AgB. Cross-linking and limited proteolysis experiments indicated different degrees of stability and compactness between the recombinant oligomers, with the AgB8/3 one showing a more stable and compact structure. We have also built AgB8 subunit structural models in order to predict the surfaces possibly involved in electrostatic and hydrophobic interactions during oligomerization.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Antigens, Helminth, Biopolymers, Chromatography, Gel, Circular Dichroism, Echinococcus granulosus, Electrostatics, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Recombinant Proteins, Sequence Homology, Amino Acid, Spectrometry, Fluorescence
Check for Full Text / PubMed Unique Identifier (PMID): 17188949
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