Structural, functional and immunological studies on a polymeric bacterial protein
The characterization of proteins from Brucella spp, the causative agent of brucellosis, has been the subject of intensive research. We have described an 18-kDa cytoplasmic protein of Brucella abortus and shown the potential usefulness of this protein as an antigen for the serologic diagnosis of bruc...
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2000
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0100879X_v33_n7_p741_Baldi http://hdl.handle.net/20.500.12110/paper_0100879X_v33_n7_p741_Baldi |
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paper:paper_0100879X_v33_n7_p741_Baldi2023-06-08T15:10:16Z Structural, functional and immunological studies on a polymeric bacterial protein Bacillus subtilis lumazine synthase Brucella lumazine synthase Brucellosis detection Immunogenicity X-ray structure Bacillus subtilis Bacteria (microorganisms) Brucella Brucella melitensis biovar Abortus Miridae 6,7 dimethyl 8 ribityllumazine synthase 6,7-dimethyl-8-ribityllumazine synthase bacterial antigen Brucella vaccine lipoprotein multienzyme complex OMP19 protein, Brucella abortus outer membrane protein recombinant protein affinity chromatography animal article Brucella abortus brucellosis chemistry crystallography enzyme linked immunosorbent assay enzymology human immunology protein quaternary structure protein tertiary structure Animals Antigens, Bacterial Bacterial Outer Membrane Proteins Brucella abortus Brucella Vaccine Brucellosis Chromatography, Affinity Crystallography Enzyme-Linked Immunosorbent Assay Humans Lipoproteins Multienzyme Complexes Protein Structure, Quaternary Protein Structure, Tertiary Recombinant Proteins The characterization of proteins from Brucella spp, the causative agent of brucellosis, has been the subject of intensive research. We have described an 18-kDa cytoplasmic protein of Brucella abortus and shown the potential usefulness of this protein as an antigen for the serologic diagnosis of brucellosis. The amino acid sequence of the protein showed a low but significant homology with that of lumazine synthases. Lumazine is an intermediate product in bacterial riboflavin biosynthesis. The recombinant form of the 18-kDa protein (expressed in E. coli) folds like the native Brucella protein and has lumazine-synthase enzymatic activity. Three-dimensional analysis by X-ray crystallography of the homolog Bacillus subtilis lumazine synthase has revealed that the enzyme forms an icosahedral capsid. Recombinant lumazine synthase from B. abortus was crystallized, diffracted X rays to 2.7-Å resolution at room temperature, and the structure successfully solved by molecular replacement procedures. The macromolecular assembly of the enzyme differs from that of the enzyme from B. subtilis. The Brucella enzyme remains pentameric (90 kDa) in its crystallographic form. Nonetheless, the active sites of the two enzymes are virtually identical at the structural level, indicating that inhibitors of these enzymes could be viable pharmaceuticals across a broad species range. We describe the structural reasons for the differences in their quaternary arrangement and also discuss the potential use of this protein as a target for the development of acellular vaccines. 2000 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0100879X_v33_n7_p741_Baldi http://hdl.handle.net/20.500.12110/paper_0100879X_v33_n7_p741_Baldi |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Bacillus subtilis lumazine synthase Brucella lumazine synthase Brucellosis detection Immunogenicity X-ray structure Bacillus subtilis Bacteria (microorganisms) Brucella Brucella melitensis biovar Abortus Miridae 6,7 dimethyl 8 ribityllumazine synthase 6,7-dimethyl-8-ribityllumazine synthase bacterial antigen Brucella vaccine lipoprotein multienzyme complex OMP19 protein, Brucella abortus outer membrane protein recombinant protein affinity chromatography animal article Brucella abortus brucellosis chemistry crystallography enzyme linked immunosorbent assay enzymology human immunology protein quaternary structure protein tertiary structure Animals Antigens, Bacterial Bacterial Outer Membrane Proteins Brucella abortus Brucella Vaccine Brucellosis Chromatography, Affinity Crystallography Enzyme-Linked Immunosorbent Assay Humans Lipoproteins Multienzyme Complexes Protein Structure, Quaternary Protein Structure, Tertiary Recombinant Proteins |
| spellingShingle |
Bacillus subtilis lumazine synthase Brucella lumazine synthase Brucellosis detection Immunogenicity X-ray structure Bacillus subtilis Bacteria (microorganisms) Brucella Brucella melitensis biovar Abortus Miridae 6,7 dimethyl 8 ribityllumazine synthase 6,7-dimethyl-8-ribityllumazine synthase bacterial antigen Brucella vaccine lipoprotein multienzyme complex OMP19 protein, Brucella abortus outer membrane protein recombinant protein affinity chromatography animal article Brucella abortus brucellosis chemistry crystallography enzyme linked immunosorbent assay enzymology human immunology protein quaternary structure protein tertiary structure Animals Antigens, Bacterial Bacterial Outer Membrane Proteins Brucella abortus Brucella Vaccine Brucellosis Chromatography, Affinity Crystallography Enzyme-Linked Immunosorbent Assay Humans Lipoproteins Multienzyme Complexes Protein Structure, Quaternary Protein Structure, Tertiary Recombinant Proteins Structural, functional and immunological studies on a polymeric bacterial protein |
| topic_facet |
Bacillus subtilis lumazine synthase Brucella lumazine synthase Brucellosis detection Immunogenicity X-ray structure Bacillus subtilis Bacteria (microorganisms) Brucella Brucella melitensis biovar Abortus Miridae 6,7 dimethyl 8 ribityllumazine synthase 6,7-dimethyl-8-ribityllumazine synthase bacterial antigen Brucella vaccine lipoprotein multienzyme complex OMP19 protein, Brucella abortus outer membrane protein recombinant protein affinity chromatography animal article Brucella abortus brucellosis chemistry crystallography enzyme linked immunosorbent assay enzymology human immunology protein quaternary structure protein tertiary structure Animals Antigens, Bacterial Bacterial Outer Membrane Proteins Brucella abortus Brucella Vaccine Brucellosis Chromatography, Affinity Crystallography Enzyme-Linked Immunosorbent Assay Humans Lipoproteins Multienzyme Complexes Protein Structure, Quaternary Protein Structure, Tertiary Recombinant Proteins |
| description |
The characterization of proteins from Brucella spp, the causative agent of brucellosis, has been the subject of intensive research. We have described an 18-kDa cytoplasmic protein of Brucella abortus and shown the potential usefulness of this protein as an antigen for the serologic diagnosis of brucellosis. The amino acid sequence of the protein showed a low but significant homology with that of lumazine synthases. Lumazine is an intermediate product in bacterial riboflavin biosynthesis. The recombinant form of the 18-kDa protein (expressed in E. coli) folds like the native Brucella protein and has lumazine-synthase enzymatic activity. Three-dimensional analysis by X-ray crystallography of the homolog Bacillus subtilis lumazine synthase has revealed that the enzyme forms an icosahedral capsid. Recombinant lumazine synthase from B. abortus was crystallized, diffracted X rays to 2.7-Å resolution at room temperature, and the structure successfully solved by molecular replacement procedures. The macromolecular assembly of the enzyme differs from that of the enzyme from B. subtilis. The Brucella enzyme remains pentameric (90 kDa) in its crystallographic form. Nonetheless, the active sites of the two enzymes are virtually identical at the structural level, indicating that inhibitors of these enzymes could be viable pharmaceuticals across a broad species range. We describe the structural reasons for the differences in their quaternary arrangement and also discuss the potential use of this protein as a target for the development of acellular vaccines. |
| title |
Structural, functional and immunological studies on a polymeric bacterial protein |
| title_short |
Structural, functional and immunological studies on a polymeric bacterial protein |
| title_full |
Structural, functional and immunological studies on a polymeric bacterial protein |
| title_fullStr |
Structural, functional and immunological studies on a polymeric bacterial protein |
| title_full_unstemmed |
Structural, functional and immunological studies on a polymeric bacterial protein |
| title_sort |
structural, functional and immunological studies on a polymeric bacterial protein |
| publishDate |
2000 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0100879X_v33_n7_p741_Baldi http://hdl.handle.net/20.500.12110/paper_0100879X_v33_n7_p741_Baldi |
| _version_ |
1768542168736071680 |