| Literature DB >> 17188949 |
Karina M Monteiro1, Sandra M N Scapin, Marcos V A S Navarro, Nilson I T Zanchin, Mateus B Cardoso, Nádya P da Silveira, Paulo F B Gonçalves, Hubert K Stassen, Arnaldo Zaha, Henrique B Ferreira.
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.Entities:
Mesh：
Substances：
Year: 2006 PMID： 17188949 DOI： 10.1016/j.bbapap.2006.11.006
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002