Role of attached lipid in immunogenicity of Borrelia burgdorferi OspA
| Autor: | Alan G. Barbour, A Sadziene, L F Erdile, G J Westrack, D J Warakomski, M A Brandt, J P Mays |
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| Jazyk: | angličtina |
| Rok vydání: | 1993 |
| Předmět: |
Lipoproteins
Immunology Molecular Sequence Data Dose-Response Relationship Immunologic Spirochaetaceae Cross Reactions Signal peptidase II Microbiology complex mixtures Immunoglobulin G Mice Antigen Animals Amino Acid Sequence Borrelia burgdorferi Cloning Molecular Lyme Disease Mice Inbred BALB C Mice Inbred C3H biology Base Sequence Immunogenicity Vaccination biology.organism_classification bacterial infections and mycoses Chromatography Ion Exchange Virology Lipids Recombinant Proteins Anti-Bacterial Agents Bacterial vaccine Infectious Diseases Humoral immunity Antigens Surface Bacterial Vaccines biology.protein Chromatography Gel bacteria Parasitology lipids (amino acids peptides and proteins) Electrophoresis Polyacrylamide Gel Peptides Protein Processing Post-Translational Research Article Bacterial Outer Membrane Proteins |
| Popis: | OspA is a protective antigen of the Lyme disease spirochete Borrelia burgdorferi. Expression of the full-length B. burgdorferi B31 OspA gene in Escherichia coli produces a protein that is processed posttranslationally by signal peptidase II and contains an attached lipid moiety. The recombinant OspA lipoprotein has been purified by detergent extraction and ion-exchange chromatography. Priming and boosting with OspA lipoprotein, either with no adjuvant or adsorbed to alum, elicited a strong, dose-dependent immunoglobulin G response. Serum from vaccinated mice inhibited spirochetal growth in vitro. Mice immunized twice with as little as 0.4 micrograms of OspA lipoprotein were protected against an intradermal challenge with 10(4) infectious spirochetes. The ability of the purified recombinant lipoprotein to induce a strong protective response in the absence of toxic adjuvants makes it an excellent candidate antigen for a human vaccine against Lyme disease. By contrast, no serum immunoglobulin G or growth inhibitory response to OspA nonlipoprotein was seen at any dose. The difference in immunogenicities of the lipoprotein and nonlipoprotein forms of OspA is not due to any difference in the antigenicities of the two proteins. These results suggest that posttranslational lipid attachment is a critical determinant of the immunogenicity of the OspA protein. |
| Databáze: | OpenAIRE |
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