A protective human monoclonal IgA antibody produced in vitro: Anti‐pneumococcal antibody engendered by Epstein‐Barr virus‐immortalized cell line
- 1 January 1986
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 16 (2) , 187-193
- https://doi.org/10.1002/eji.1830160214
Abstract
Human lymphocytes that produce anti-pneumococcal antibodies were separated and immortalized by Epstein-Barr virus and then cloned. One clone (NAD-Sel) produces an IgA, x antibody which is specific for the polysaccharides of type 8 pneumococcus, while not reactive with any of the polysaccharides derived from 24 other pneumococcal strains. The antibody, which is present in the cell supernatant as monomer and polymer, binds to protein A and does not fix complement. When incubated in vitro with type 8 pneumococci, it induces direct killing and increases the opsonization of these bacteria by mouse macrophages.This publication has 25 references indexed in Scilit:
- Binding of Human IgA Fragments to Protein A-Sepharose Studied with an ELISA MethodScandinavian Journal of Immunology, 1985
- Continuous in vitro production of IgA by a human colostral immortalized cell lineImmunology Letters, 1985
- Human monoclonal antibodies produced by Epstein-Barr virus transformed cell lines bind protein AImmunology Letters, 1985
- Human lymphoblastoid cell line producing protective monoclonal IgG1, χ anti‐tetanus toxinEuropean Journal of Immunology, 1984
- Herpes Simplex Virus Glycoprotein D: Human Monoclonal Antibody Produced by Bone Marrow Cell LineScience, 1983
- Production of Human Monoclonal Antibody to X31 Influenza Virus NucleoproteinJournal of General Virology, 1983
- Human monoclonal antibodies produced by immortalization with Epstein-Barr virusImmunology Today, 1981
- EB virus-induced B lymphocyte cell lines producing specific antibodyNature, 1977
- A plaque assay for all cells secreting Ig of a given type or classEuropean Journal of Immunology, 1976
- Enzyme-linked immunosorbent assay (ELISA) quantitative assay of immunoglobulin GImmunochemistry, 1971