Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

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Protein assemblies with a high degree of repetitiveness and organization are known to induce strong immune responses. For that reason they have been postulated for the design of subunit vaccines by means of protein engineering. The enzyme lumazine synthase from Brucella spp. (BLS) is highly immunoge...

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Autores principales:	Laplagne, D.A., Zylberman, V., Ainciart, N., Steward, M.W., Sciutto, E., Fossati, C.A., Goldbaum, F.A.
Formato:	JOUR
Materias:	Chimeric protein Decamer Immunogenicity Multiple display of peptides Polyvalent chimeras Stability bacterial enzyme bacterial protein chimeric protein lumazine synthase peptide subunit vaccine unclassified drug article Brucella chimera immune response immune system nonhuman polymerization priority journal protein assembly protein engineering protein folding protein stability stoichiometry structure analysis thermodynamics Amino Acid Sequence Animals Bacterial Proteins Biopolymers Circular Dichroism Gene Expression Genetic Vectors Mice Mice, Inbred BALB C Models, Molecular Molecular Sequence Data Multienzyme Complexes Peptide Library Protein Engineering Protein Folding Recombinant Fusion Proteins Bacteria (microorganisms)
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_08873585_v57_n4_p820_Laplagne
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_08873585_v57_n4_p820_Laplagne
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spelling	todo:paper_08873585_v57_n4_p820_Laplagne2023-10-03T15:40:49Z Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides Laplagne, D.A. Zylberman, V. Ainciart, N. Steward, M.W. Sciutto, E. Fossati, C.A. Goldbaum, F.A. Chimeric protein Decamer Immunogenicity Multiple display of peptides Polyvalent chimeras Stability bacterial enzyme bacterial protein chimeric protein lumazine synthase peptide subunit vaccine unclassified drug article Brucella chimera immune response immune system nonhuman polymerization priority journal protein assembly protein engineering protein folding protein stability stoichiometry structure analysis thermodynamics Amino Acid Sequence Animals Bacterial Proteins Biopolymers Brucella Circular Dichroism Gene Expression Genetic Vectors Mice Mice, Inbred BALB C Models, Molecular Molecular Sequence Data Multienzyme Complexes Peptide Library Protein Engineering Protein Folding Recombinant Fusion Proteins Bacteria (microorganisms) Brucella Protein assemblies with a high degree of repetitiveness and organization are known to induce strong immune responses. For that reason they have been postulated for the design of subunit vaccines by means of protein engineering. The enzyme lumazine synthase from Brucella spp. (BLS) is highly immunogenic, presumably owing to its homodecameric arrangement and remarkable thermodynamic stability. Structural analysis has shown that it is possible to insert foreign peptides at the ten amino terminus of BLS without disrupting its general folding. These peptides would be displayed to the immune system in a highly symmetric three-dimensional array. In the present work, BLS has been used as a protein carrier of foreign peptides. We have established a modular system to produce chimeric proteins decorated with ten copies of a desired peptide as long as 27 residues and have shown that their folding and stability is similar to that of the wild-type protein. The knowledge about the mechanisms of dissociation and unfolding of BLS allowed the engineering of polyvalent chimeras displaying different predefined peptides on the same molecular scaffold. Moreover, the reassembly of mixtures of chimeras at different steps of the unfolding process was used to control the stoichiometry and spatial arrangement for the simultaneous display of different peptides on BLS. This strategy would be useful for vaccine development and other biomedical applications. © 2004 Wiley-Liss, Inc. Fil:Laplagne, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Zylberman, V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ainciart, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_08873585_v57_n4_p820_Laplagne
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Chimeric protein Decamer Immunogenicity Multiple display of peptides Polyvalent chimeras Stability bacterial enzyme bacterial protein chimeric protein lumazine synthase peptide subunit vaccine unclassified drug article Brucella chimera immune response immune system nonhuman polymerization priority journal protein assembly protein engineering protein folding protein stability stoichiometry structure analysis thermodynamics Amino Acid Sequence Animals Bacterial Proteins Biopolymers Brucella Circular Dichroism Gene Expression Genetic Vectors Mice Mice, Inbred BALB C Models, Molecular Molecular Sequence Data Multienzyme Complexes Peptide Library Protein Engineering Protein Folding Recombinant Fusion Proteins Bacteria (microorganisms) Brucella
spellingShingle	Chimeric protein Decamer Immunogenicity Multiple display of peptides Polyvalent chimeras Stability bacterial enzyme bacterial protein chimeric protein lumazine synthase peptide subunit vaccine unclassified drug article Brucella chimera immune response immune system nonhuman polymerization priority journal protein assembly protein engineering protein folding protein stability stoichiometry structure analysis thermodynamics Amino Acid Sequence Animals Bacterial Proteins Biopolymers Brucella Circular Dichroism Gene Expression Genetic Vectors Mice Mice, Inbred BALB C Models, Molecular Molecular Sequence Data Multienzyme Complexes Peptide Library Protein Engineering Protein Folding Recombinant Fusion Proteins Bacteria (microorganisms) Brucella Laplagne, D.A. Zylberman, V. Ainciart, N. Steward, M.W. Sciutto, E. Fossati, C.A. Goldbaum, F.A. Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides
topic_facet	Chimeric protein Decamer Immunogenicity Multiple display of peptides Polyvalent chimeras Stability bacterial enzyme bacterial protein chimeric protein lumazine synthase peptide subunit vaccine unclassified drug article Brucella chimera immune response immune system nonhuman polymerization priority journal protein assembly protein engineering protein folding protein stability stoichiometry structure analysis thermodynamics Amino Acid Sequence Animals Bacterial Proteins Biopolymers Brucella Circular Dichroism Gene Expression Genetic Vectors Mice Mice, Inbred BALB C Models, Molecular Molecular Sequence Data Multienzyme Complexes Peptide Library Protein Engineering Protein Folding Recombinant Fusion Proteins Bacteria (microorganisms) Brucella
description	Protein assemblies with a high degree of repetitiveness and organization are known to induce strong immune responses. For that reason they have been postulated for the design of subunit vaccines by means of protein engineering. The enzyme lumazine synthase from Brucella spp. (BLS) is highly immunogenic, presumably owing to its homodecameric arrangement and remarkable thermodynamic stability. Structural analysis has shown that it is possible to insert foreign peptides at the ten amino terminus of BLS without disrupting its general folding. These peptides would be displayed to the immune system in a highly symmetric three-dimensional array. In the present work, BLS has been used as a protein carrier of foreign peptides. We have established a modular system to produce chimeric proteins decorated with ten copies of a desired peptide as long as 27 residues and have shown that their folding and stability is similar to that of the wild-type protein. The knowledge about the mechanisms of dissociation and unfolding of BLS allowed the engineering of polyvalent chimeras displaying different predefined peptides on the same molecular scaffold. Moreover, the reassembly of mixtures of chimeras at different steps of the unfolding process was used to control the stoichiometry and spatial arrangement for the simultaneous display of different peptides on BLS. This strategy would be useful for vaccine development and other biomedical applications. © 2004 Wiley-Liss, Inc.
format	JOUR
author	Laplagne, D.A. Zylberman, V. Ainciart, N. Steward, M.W. Sciutto, E. Fossati, C.A. Goldbaum, F.A.
author_facet	Laplagne, D.A. Zylberman, V. Ainciart, N. Steward, M.W. Sciutto, E. Fossati, C.A. Goldbaum, F.A.
author_sort	Laplagne, D.A.
title	Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides
title_short	Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides
title_full	Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides
title_fullStr	Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides
title_full_unstemmed	Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides
title_sort	engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides
url	http://hdl.handle.net/20.500.12110/paper_08873585_v57_n4_p820_Laplagne
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Engineering of a polymeric bacterial protein as a scaffold for the multiple display of peptides

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