Characterization of structural and ...
Document type :
Article dans une revue scientifique: Article original
DOI :
PMID :
Title :
Characterization of structural and immunological properties of a fusion protein between flagellin from Salmonella and lumazine synthase from Brucella.
Author(s) :
Hiriart, Y. [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Rossi, A. H. [Auteur]
Fundación Instituto Leloir [Buenos Aires]
Biedma, M [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Errea, J. [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Moreno, G. [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Cayet, D. [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Rinaldi, J. [Auteur]
Fundación Instituto Leloir [Buenos Aires]
Blancá, B. [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Sirard, J. C. [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Goldbaum, F [Auteur]
Fundación Instituto Leloir [Buenos Aires]
Berguer, P [Auteur]
Fundación Instituto Leloir [Buenos Aires]
Rumbo, M [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Rossi, A. H. [Auteur]
Fundación Instituto Leloir [Buenos Aires]
Biedma, M [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Errea, J. [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Moreno, G. [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Cayet, D. [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Rinaldi, J. [Auteur]
Fundación Instituto Leloir [Buenos Aires]
Blancá, B. [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Sirard, J. C. [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Goldbaum, F [Auteur]
Fundación Instituto Leloir [Buenos Aires]
Berguer, P [Auteur]
Fundación Instituto Leloir [Buenos Aires]
Rumbo, M [Auteur]
Instituto de Estudios Inmunológicos y Fisiopatológicos [Buenos Aires, Argentina] [IIPF]
Journal title :
Protein Science
Pages :
1049-1059
Publisher :
Wiley
Publication date :
2017-03-16
ISSN :
0961-8368
English keyword(s) :
BLS
TLR5
flagellin
scaffold
TLR5
flagellin
scaffold
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
Aiming to combine the flexibility of Brucella lumazine synthase (BLS) to adapt different protein domains in a decameric structure and the capacity of BLS and flagellin to enhance the immunogenicity of peptides that are ...
Show more >Aiming to combine the flexibility of Brucella lumazine synthase (BLS) to adapt different protein domains in a decameric structure and the capacity of BLS and flagellin to enhance the immunogenicity of peptides that are linked to their structure, we generated a chimeric protein (BLS-FliC131) by fusing flagellin from Salmonella in the N-termini of BLS. The obtained protein was recognized by anti-flagellin and anti-BLS antibodies, keeping the oligomerization capacity of BLS, without affecting the folding of the monomeric protein components determined by circular dichroism. Furthermore, the thermal stability of each fusion partner is conserved, indicating that the interactions that participate in its folding are not affected by the genetic fusion. Besides, either in vitro or in vivo using TLR5-deficient animals we could determine that BLS-FliC131 retains the capacity of triggering TLR5. The humoral response against BLS elicited by BLS-FliC131 was stronger than the one elicited by equimolar amounts of BLS + FliC. Since BLS scaffold allows the generation of hetero-decameric structures, we expect that flagellin oligomerization on this protein scaffold will generate a new vaccine platform with enhanced capacity to activate immune responses.Show less >
Show more >Aiming to combine the flexibility of Brucella lumazine synthase (BLS) to adapt different protein domains in a decameric structure and the capacity of BLS and flagellin to enhance the immunogenicity of peptides that are linked to their structure, we generated a chimeric protein (BLS-FliC131) by fusing flagellin from Salmonella in the N-termini of BLS. The obtained protein was recognized by anti-flagellin and anti-BLS antibodies, keeping the oligomerization capacity of BLS, without affecting the folding of the monomeric protein components determined by circular dichroism. Furthermore, the thermal stability of each fusion partner is conserved, indicating that the interactions that participate in its folding are not affected by the genetic fusion. Besides, either in vitro or in vivo using TLR5-deficient animals we could determine that BLS-FliC131 retains the capacity of triggering TLR5. The humoral response against BLS elicited by BLS-FliC131 was stronger than the one elicited by equimolar amounts of BLS + FliC. Since BLS scaffold allows the generation of hetero-decameric structures, we expect that flagellin oligomerization on this protein scaffold will generate a new vaccine platform with enhanced capacity to activate immune responses.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Source :
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- https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5405423/pdf
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