Activity of human IgG and IgA subclasses in immune defense against Neisseria meningitidis serogroup B
Autor: | Mohamed R. Daha, Henriette A. Vilé, Matthijs Jansen, J. M. H. van Den Elsen, H. C. Morton, Blaise Corthésy, E Boel, Gestur Vidarsson, J.G.J. van de Winkel, W. L. van der Pol, J. Duijs |
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Přispěvatelé: | Academic Medical Center, Landsteiner Laboratory |
Jazyk: | angličtina |
Rok vydání: | 2001 |
Předmět: |
Immune defense
Blood Bactericidal Activity Secretory component Neutrophils Phagocytosis Recombinant Fusion Proteins Immunology Porins Receptors Fc Biology Neisseria meningitidis medicine.disease_cause Microbiology Cell Line Bacteriolysis Cricetinae Baby hamster kidney cell medicine Immunology and Allergy Animals Humans Complement Activation Respiratory Burst J chain Immunity Innate Respiratory burst Immunoglobulin A Immunoglobulin G Porin Immunoglobulin A Secretory Binding Sites Antibody Dimerization |
Zdroj: | Journal of immunology (Baltimore, Md., 166(10), 6250-6256. American Association of Immunologists |
ISSN: | 0022-1767 |
Popis: | Both IgG and IgA Abs have been implicated in host defense against bacterial infections, although their relative contributions remain unclear. We generated a unique panel of human chimeric Abs of all human IgG and IgA subclasses with identical V genes against porin A, a major subcapsular protein Ag of Neisseria meningitidis and a vaccine candidate. Chimeric Abs were produced in baby hamster kidney cells, and IgA-producing clones were cotransfected with human J chain and/or human secretory component. Although IgG (isotypes IgG1–3) mediated efficient complement-dependent lysis, IgA was unable to. However, IgA proved equally active to IgG in stimulating polymorphonuclear leukocyte respiratory burst. Remarkably, although porin-specific monomeric, dimeric, and polymeric IgA triggered efficient phagocytosis, secretory IgA did not. These studies reveal unique and nonoverlapping roles for IgG and IgA Abs in defense against meningococcal infections. |
Databáze: | OpenAIRE |
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