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Self-assembly and structural characterization of Echinococcus granulosus antigen B recombinant subunit oligomers

2006; Elsevier BV; Volume: 1774; Issue: 2 Linguagem: Inglês

10.1016/j.bbapap.2006.11.006

1878-1454

Karina Mariante Monteiro, Sandra Mara Naressi Scapin, M.V.A.S. Navarro, Nilson Ivo Tonin Zanchin, Mateus Borba Cardoso, Nádya Pesce da Silveira, Paulo Fernando Bruno Gonçalves, Hubert Stassen, Arnaldo Zaha, Henrique Bunselmeyer Ferreira,

Trace Elements in Health

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 ~ 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.