Hybrid IgA2/IgG1 antibodies with tailor-made effector functions
Copyright 2001 Academic Press.
| Veröffentlicht in: | Clinical immunology (Orlando, Fla.). - 1999. - 101(2001), 1 vom: 28. Okt., Seite 21-31 |
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| Weitere Verfasser: | , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2001
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| Zugriff auf das übergeordnete Werk: | Clinical immunology (Orlando, Fla.) |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Histocompatibility Antigens Class I Immunoglobulin A Immunoglobulin Constant Regions Immunoglobulin G Receptors, Fc Receptors, IgG Receptors, Polymeric Immunoglobulin mehr... |
| Zusammenfassung: | Copyright 2001 Academic Press. Immunoglobulin (Ig) A and IgG are the principal immune effector molecules at mucosal surfaces and in blood, respectively. Mucosal IgA is polymeric and bound to secretory component, whereas serum IgG is monomeric. We have now produced IgA2/IgG1 hybrid antibodies that combine the properties of IgA and IgG. Antibodies with Calpha3 at the end of the IgG H chain resemble IgA and form polymers with J chain that bind the polymeric Ig receptor. Like IgG, the hybrid proteins activated complement and bound FcgammaRI and protein A. Though the hybrid proteins contained both Cgamma2 and Cgamma3, they have a short in vivo half-life. Surprisingly, this decreased half-life correlated with a higher avidity than that of IgG for murine FcRn. Interestingly, antibodies with Calpha1 replacing Cgamma1 were resistant to extremes of pH, suggesting that Calpha1 increases antibody stability. These results provide insights into engineering antibodies with novel combinations of effector functions |
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| Beschreibung: | Date Completed 04.12.2001 Date Revised 30.11.2018 published: Print Citation Status MEDLINE |
| ISSN: | 1521-7035 |