Antibodies to Polysialic Acid and its N-Propyl Derivative: Binding Properties and Interaction with Human Embryonal Brain Glycopeptides

There is no efficient vaccine against group B meningococcal meningitis because of tolerance induced by host tissue polysialic acid cross-reacting with the capsular polysaccharide. The specificities of polysialic acid-antibody interactions were studied using a ligand binding assay. Antibodies 735, 20...

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Bibliographic Details
Published in:The Journal of infectious diseases 1995-06, Vol.171 (6), p.1481-1490
Main Authors: Häyrinen, Jukka, Jennings, Harold, Raff, Howard V., Rougon, Geneviève, Hanai, Nobuo, Gerardy-Schahn, Rita, Finne, Jukka
Format: Article
Language:English
Subjects:
Antibodies
Antibodies, Monoclonal - immunology
Antibody Specificity
Antigens
Bacterial Vaccines - immunology
Bacteriology
Biological and medical sciences
Brain - embryology
Brain - immunology
Cross Reactions
Fundamental and applied biological sciences. Psychology
Gangliosides
Glycopeptides
Glycopeptides - immunology
Humans
Ligands
Major Articles
Microbiology
Monoclonal antibodies
Neisseria meningitidis
Neural cell adhesion molecules
Polysaccharides
Polysaccharides - immunology
Polysaccharides, Bacterial - immunology
Propionates
Sialic Acids - chemistry
Sialic Acids - immunology
Vaccination
Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies
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Summary:There is no efficient vaccine against group B meningococcal meningitis because of tolerance induced by host tissue polysialic acid cross-reacting with the capsular polysaccharide. The specificities of polysialic acid-antibody interactions were studied using a ligand binding assay. Antibodies 735, 20-1, 2-1B, 2-2B, 5El, and t5El and antibodies against N-propionylated group B meningococcal polysaccharide-tetanus toxoid conjugate (NP-4, 106-6) bound polysialylated human embryonal brain glycopeptides but not control glycopeptides or disialosyllactose, whereas antibodies 109-3 and 1-627 were more specific for the N-propionylated polysaccharide. Antiganglioside antibodies (KM538, KM641) did not cross-react with polysialic acid. Human classs-witched antibodies 5El (IgM) and t5El (lgG) reacted identically with all compounds tested and no temperature-dependent differences were observed. All anti-polysialosyl antibodies required a polysaccharide chain of 8-10 residues for binding independent of the immunizing antigen, animal species, or immunoglobulin class. The results suggest careful evaluation of polysialic acid cross-reactivity in vaccine development.
ISSN:0022-1899
1537-6613
DOI:10.1093/infdis/171.6.1481