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Published online before print April 1, 2004
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RIIa expression with FcRI results in C-reactive protein- and IgG-mediated phagocytosis
* Immunology Unit, Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, United Kingdom; and
Department of Physiology, University College, Cork, Ireland
1 Correspondence at current address: School of Biomedical and Molecular Sciences, University of Surrey, Guildford, Surrey GU2 7HX, UK. E-mail: k.bodman-smith{at}surrey.ac.uk
C-reactive protein (CRP) is a pattern-recognition molecule, which can bind to phosphorylcholine and certain phosphorylated carbohydrates found on the surface of a number of microorganisms. CRP has been shown recently to bind human Fc receptor for immunoglobulin G (IgG; Fc
R)I and mediate phagocytosis and signaling through the -chain. To date, binding of monomeric CRP to FcRII has been contentious. We demonstrate that erythrocytes opsonized with CRP bind FcRIIa-transfected COS-7 cells. In addition, we demonstrate that FcRI can use FcRIIa R131 and H131 to phagocytose erythrocytes coated with IgG or purified or recombinant CRP in the absence of the -chain. COS-7 cells expressing FcRIIa or FcRI alone did not phagocytose opsonized erythrocytes. Such phagocytosis required the cytoplasmic domain of FcRIIa, as mutation of tyrosine at position 205 and truncation of the cytoplasmic domain from the end of the transmembrane region (position 206), resulting in the loss of the immunoreceptor tyrosine activatory motif, abrogated phagocytosis. FcRIIa R131 was more efficient than FcRIIa H131 at mediating CRP-dependent phagocytosis.
Key Words: pentraxin • Fc receptors • phosphorylcholine • COS-7
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