Incomplete protection of hamsters vaccinated with unlipidated OspA from Borrelia burgdorferi infection is associated with low levels of antibody to an epitope defined by mAb LA-2
Efforts to develop a recombinant vaccine for Lyme disease have focused on using the outer surface protein A (OspA) of Borrelia burgdorferi as an immunogen. We evaluated the effectiveness of an unlipidated recombinant OspA as a vaccine in hamsters. This molecule is soluble and can be produced in high...
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Published in | Vaccine Vol. 13; no. 12; pp. 1086 - 1094 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford
Elsevier Ltd
01.08.1995
Elsevier |
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Abstract | Efforts to develop a recombinant vaccine for Lyme disease have focused on using the outer surface protein A (OspA) of
Borrelia burgdorferi as an immunogen. We evaluated the effectiveness of an unlipidated recombinant OspA as a vaccine in hamsters. This molecule is soluble and can be produced in high yield in
Escherichia coli, characteristics that permit simple and relatively low cost production. Vaccination with unlipidated OspA protected a substantial portion of animals—59–79%, depending on the challenge strain and route—against moderate doses of spirochetes delivered either by injection or by bite of infected nymphal ticks (
Ixodes scapularis). The instances of vaccine failure were associated with development of low levels of antibody to a particular OspA epitope, one defined by mAb LA-2. At least 50 ng ml
−1 of LA-2 equivalent antibody was necessary for protection of hamsters. Lower LA-2 equivalent antibody concentrations occurred in unprotected animals in the presence of high-titered polyclonal antibody to native OspA. A competitive binding assay to quantitate this serum fraction is described that should be of use in monitoring the quality of the antibody response to OspA in vaccine trials. Concentrations of LA-2 equivalent antibody parallel the ability of the serum specimens to inhibit the growth of
B. burgdorferi in culture. |
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AbstractList | Efforts to develop a recombinant vaccine for Lyme disease have focused on using the outer surface protein A (OspA) of Borrelia burgdorferi as an immunogen. We evaluated the effectiveness of an unlipidated recombinant OspA as a vaccine in hamsters. This molecule is soluble and can be produced in high yield in Escherichia coli, characteristics that permit simple and relatively low cost production. Vaccination with unlipidated OspA protected a substantial portion of animals--59-79%, depending on the challenge strain and route--against moderate doses of spirochetes delivered either by injection or by bite of infected nymphal ticks (Ixodes scapularis). The instances of vaccine failure were associated with development of low levels of antibody to a particular OspA epitope, one defined by mAb LA-2. At least 50 ng ml-1 of LA-2 equivalent antibody was necessary for protection of hamsters. Lower LA-2 equivalent antibody concentrations occurred in unprotected animals in the presence of high-titered polyclonal antibody to native OspA. A competitive binding assay to quantitate this serum fraction is described that should be of use in monitoring the quality of the antibody response to OspA in vaccine trials. Concentrations of LA-2 equivalent antibody parallel the ability of the serum specimens to inhibit the growth of B. burgdorferi in culture. Efforts to develop a recombinant vaccine for Lyme disease have focused on using the outer surface protein A (OspA) of Borrelia burgdorferi as an immunogen. We evaluated the effectiveness of an unlipidated recombinant OspA as a vaccine in hamsters. This molecule is soluble and can be produced in high yield in Escherichia coli, characteristics that permit simple and relatively low cost production. Vaccination with unlipidated OspA protected a substantial portion of animals—59–79%, depending on the challenge strain and route—against moderate doses of spirochetes delivered either by injection or by bite of infected nymphal ticks ( Ixodes scapularis). The instances of vaccine failure were associated with development of low levels of antibody to a particular OspA epitope, one defined by mAb LA-2. At least 50 ng ml −1 of LA-2 equivalent antibody was necessary for protection of hamsters. Lower LA-2 equivalent antibody concentrations occurred in unprotected animals in the presence of high-titered polyclonal antibody to native OspA. A competitive binding assay to quantitate this serum fraction is described that should be of use in monitoring the quality of the antibody response to OspA in vaccine trials. Concentrations of LA-2 equivalent antibody parallel the ability of the serum specimens to inhibit the growth of B. burgdorferi in culture. Efforts to develop a recombinant vaccine for Lyme disease have focused on using the outer surface protein A (OspA) of Borrelia burgdorferi as an immunogen. We evaluated the effectiveness of an unlipidated recombinant OspA as a vaccine in hamsters. This molecule is soluble and can be produced in high yield in Escherichia coli, characteristics that permit simple and relatively low cost production. Vaccination with unlipidated OspA protected a substantial portion of animals-59-79%, depending on the challenge strain and route-against moderate doses of spirochetes delivered either by injection or by bite of infected nymphal ticks (Ixodes scapularis). The instances of vaccine failure were associated with development of low levels of antibody to a particular OspA epitope, one defined by mAb LA-2. At least 50 ng ml super(-1) of LA-2 equivalent antibody was necessary for protection of hamsters. Lower LA-2 equivalent antibody concentrations occurred in unprotected animals in the presence of high-titered polyclonal antibody to native OspA. A competitive binding assay to quantitate this serum fraction is described that should be of use in monitoring the quality of the antibody response to OspA in vaccine trials. Concentrations of LA-2 equivalent antibody parallel the ability of the serum specimens to inhibit the growth of B. burgdorferi in culture. |
Author | Mayer, Leonard W. Piesman, Joseph Johnson, Barbara J.B. Sviat, Steven L. Happ, Christine M. Dunn, John J. Frantz, Joseph C. |
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Keywords | outer surface protein Lyme disease Borrelia burgdorferi vaccine LA-2 antibody Immune response Spirochaetaceae Spirochaetales Antigenic determinant Rodentia Borrelia infection Vaccine Cell surface Infection Vertebrata Mammalia Immunogenicity Bacteriosis Bacteria Hamster Humoral immunity Spirachaetosis |
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Snippet | Efforts to develop a recombinant vaccine for Lyme disease have focused on using the outer surface protein A (OspA) of
Borrelia burgdorferi as an immunogen. We... Efforts to develop a recombinant vaccine for Lyme disease have focused on using the outer surface protein A (OspA) of Borrelia burgdorferi as an immunogen. We... |
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SubjectTerms | Animals Antibodies, Bacterial - blood Antibodies, Monoclonal - immunology Antigens, Surface - immunology Bacterial Outer Membrane Proteins - immunology Bacterial Vaccines - immunology Bacteriology Biological and medical sciences Borrelia burgdorferi Borrelia burgdorferi Group - immunology Cricetinae Epitopes Female Fundamental and applied biological sciences. Psychology hamster LA-2 antibody Lipoproteins Lyme disease Lyme Disease - prevention & control Mesocricetus Microbiology outer surface protein Vaccination vaccine Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies Vaccines, Synthetic - immunology |
Title | Incomplete protection of hamsters vaccinated with unlipidated OspA from Borrelia burgdorferi infection is associated with low levels of antibody to an epitope defined by mAb LA-2 |
URI | https://dx.doi.org/10.1016/0264-410X(95)00035-Y https://www.ncbi.nlm.nih.gov/pubmed/7491816 https://search.proquest.com/docview/16873092 https://search.proquest.com/docview/77724438 |
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