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A monoclonal antibody specific for immunoglobulin A receptor triggers polymorphonuclear neutrophil superoxide release
Author(s) -
Shen Li
Publication year - 1992
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.51.4.373
Subject(s) - respiratory burst , fc receptor , monoclonal antibody , receptor , superoxide , antibody , microbiology and biotechnology , cd64 , immunoglobulin g , biology , immunology , immunoglobulin fc fragments , immunoglobulin a , cd16 , antigen , biochemistry , cd3 , cd8 , enzyme
An immunoglobulin M (IgM) monoclonal antibody, My43, specific for IgA Fc receptor (FcαR) on human monocytes, bound to human polymorphonuclear neutrophils (PMNs) and inhibited their ability to bind IgA but not IgG. It was observed that the PMN oxidative burst was induced by both polymeric IgA and aggregated IgG, whereas IgM was without effect. The IgG‐mediated oxidative burst was inhibited by anti‐FcγRII Fab and anti‐FcγRIII F(ab') 2 but not by My43. Conversely, the IgA‐mediated oxidative burst was inhibited by My43 but not by anti‐FcγRII or anti‐FcγRIII. When anti‐Fc receptor monoclonal antibodies (mAbs) were used directly as ligands, it was observed that both anti‐FcγRII Fab and anti‐FcγRII F(ab') 2 promoted the oxidative burst when cross‐linked. Moreover, My43, when cross‐linked with F(ab') 2 antimouse IgM, also triggered the oxidative burst, whereas an IgM anti‐GDI5 mAb, PM81, did not stimulate function. This demonstrates that IgA receptors on PMNs are function‐triggering molecules and that an anti‐IgA receptor mAb may be substituted as a ligand.