http://www.cnr.it/ontology/cnr/individuo/prodotto/ID271766
A Structure-Based Strategy for Epitope Discovery in Burkholderia pseudomallei OppA Antigen (Articolo in rivista)
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- Label
- A Structure-Based Strategy for Epitope Discovery in Burkholderia pseudomallei OppA Antigen (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.str.2012.10.005 (literal)
- Alternative label
Lassaux, Patricia; Peri, Claudio; Ferrer-Navarro, Mario; Gourlay, Louise J.; Gori, Alessandro; Conchillo-Sole, Oscar; Rinchai, Darawan; Lertmemongkolchai, Ganjana; Longhi, Renato; Daura, Xavier; Colombo, Giorgio; Bolognesi, Martino (2013)
A Structure-Based Strategy for Epitope Discovery in Burkholderia pseudomallei OppA Antigen
in Structure (Lond.)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Lassaux, Patricia; Peri, Claudio; Ferrer-Navarro, Mario; Gourlay, Louise J.; Gori, Alessandro; Conchillo-Sole, Oscar; Rinchai, Darawan; Lertmemongkolchai, Ganjana; Longhi, Renato; Daura, Xavier; Colombo, Giorgio; Bolognesi, Martino (literal)
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- ISI Web of Science (WoS) (literal)
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- University of Milan; Consiglio Nazionale delle Ricerche (CNR); Consiglio Nazionale delle Ricerche (CNR); Autonomous University of Barcelona; Khon Kaen University; Catalan Inst Res & Adv Studies (literal)
- Titolo
- A Structure-Based Strategy for Epitope Discovery in Burkholderia pseudomallei OppA Antigen (literal)
- Abstract
- We present an approach integrating structural and computational biology with immunological tests to identify epitopes in the OppA antigen from the Gram-negative pathogen Burkholderia pseudomallei, the etiological agent of melioidosis. The crystal structure of OppA(Bp), reported here at 2.1 angstrom resolution, was the basis for a computational analysis that identified three potential epitopes. In parallel, antigen proteolysis and immunocapturing allowed us to identify three additional peptides. All six potential epitopes were synthesized as free peptides and tested for their immunoreactivity against sera from healthy seronegative, healthy seropositive, and recovered melioidosis patients. Three synthetic peptides allowed the different patient groups to be distinguished, underlining the potential of this approach. Extension of the computational analysis, including energy-based decomposition methods, allowed rationalizing results of the predictive analyses and the immunocapture epitope mapping. Our results illustrate a structure-based epitope discovery process, whose application may expand our perspectives in the diagnostic and vaccine design fields. (literal)
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