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The Journal of Immunology, 1998, 160: 20-23.
Copyright © 1998 by The American Association of Immunologists

CUTTING EDGE

Cutting Edge: Identification of the Mouse IgG3 Receptor: Implications for Antibody Effector Function at the Interface Between Innate and Adaptive Immunity

Amanda L. Gavin, Nadine Barnes, Hilde M. Dijstelbloem and P. Mark Hogarth1

The Austin Research Institute, Austin and Repatriation Medical Centre, Heidelberg, Victoria, Australia


   Abstract
Top
 Abstract
Introduction
 Materials and Methods
 Results and Discussion
 References
 
Mouse IgG3 appears early in immune responses independently of T cell help and, as such, is an early effector molecule of the immune system. Yet, a specific IgG3 cellular receptor remains undefined. In transfection experiments, mouse Fc{gamma}RI was clearly able to bind immune complexes of IgG3, whereas mouse Fc{gamma}RII could not. Furthermore, macrophages from mice expressing Fc{gamma}RII and Fc{gamma}RIII but lacking Fc{gamma}RI were unable to phagocytose IgG3 immune complexes, thus identifying mouse Fc{gamma}RI as the sole receptor for IgG3 immune complexes. Competition studies demonstrated that monomeric mouse IgG3 could inhibit IgG2a binding to mouse Fc{gamma}RI with an ID50 {approx}10-7 M (fivefold lower than IgG2a). The identification of mouse Fc{gamma}RI as the IgG3 receptor establishes Fc{gamma}RI as a participant in events at the interface between innate and adaptive immunity, implying a greater role for this receptor in the development of normal and pathologic immune responses than previously recognized.


   Introduction
Top
 Abstract
 Introduction
Materials and Methods
 Results and Discussion
 References
 
Mouse IgG3, which is not a homologue of human IgG3, is the only T cell-independent IgG subclass and has a number of unique properties (1, 2, 3, 4). The specificity of this IgG is directed primarily against carbohydrates and repeating epitope Ags and, by nature of its self-associating properties, can elicit powerful effector function early in immune responses (5, 6, 7). IgG3 is important in the resistance to pathogens (8) and is involved in pathogenic processes in autoimmune disease, especially immune complex precipitation and glomerulonephritis (5, 9, 10, 11, 12). A cellular receptor for mouse IgG3, however, has remained undefined.

Diamond and Yelton proposed that a new, previously unidentified IgG3 Fc receptor might exist on the surface of macrophages (13). More recently, the molecular cloning of the three defined IgG Fc receptors, Fc{gamma}RI, Fc{gamma}RII, and Fc{gamma}RIII, and the binding specificity analyses conducted on these receptors in isolation, however, have failed to identify the IgG3 binding receptor of mouse macrophages.

This study identifies mouse Fc{gamma}RI as the IgG3 receptor of macrophages and shows that although Fc{gamma}RI is a "high affinity" receptor for IgG2a, it binds IgG3 with at least fivefold lower affinity.


   Materials and Methods
Top
 Abstract
 Introduction
 Materials and Methods
Results and Discussion
 References
 
Ab reagents

The following Abs were used as either tissue culture supernatant or protein A-purified IgG from culture supernatant: UM1, UM2a, and UM3 (anti-trinitrophenyl (TNP),2 and mouse IgG1, IgG2a, and IgG3, respectively) (14); 49-31.1 (anti-Ly2.1, mIgG3) (15); 5119-4 (anti-Ly6B.2, mIgG3) (16); 7-20.6/3 (anti-Ly1.1, mIgG2a) (17); 49-11.1 (anti-Ly2.1, mIgG2a); 49-14.1 (anti-Ly2.1, mIgG1) (15); 49.2 (anti-TNP, IgG2b) (PharMingen, San Diego, CA). UM1, UM2a, and UM3 were kind gifts from Dr. Tohru Masuda (Kyoto University, Kyoto, Japan). Purified Abs were stored at -80°C and thawed once only for use. Analytical gel filtration (Superdex-200, Pharmacia, Uppsala, Sweden) routinely showed that the Ab preparations used were 90–95% monomer.

Transfection of Fc{gamma}R cDNA constructs

CHO-K1 cells stably expressing mouse Fc{gamma}RI (1N3-2) were generated by CaP04 transfection of the expression vector pCDNA3 (Invitrogen, Carlsbad, CA) containing mouse Fc{gamma}RI cDNA (18). This construct, Fc{gamma}RI-BALB-pCDNA3, and mouse Fc{gamma}RIIb1 cDNA (19), subcloned into the expression vector pKC4 (20), were transiently expressed by COS cells (21). The efficiency of transient transfection and expression was approximately 30 to 50% for mouse Fc{gamma}RI, with mouse Fc{gamma}RII expression slightly lower (20%).

Experimental mice

All mice used were housed at the Austin Research Institute animal-holding facility. Mice lacking Fc{gamma}RI expression were generated by homologous recombination and bred to homozygosity at the fcgrI null allele (manuscript in preparation N. Barnes, A. L. Gavin, P. S. Tan, and P. M. Hogarth).

Bone marrow-derived macrophages (BMM)

BMM (95% F4/80+) were generated as adherent cells from their nonadherent progenitors, essentially as described (22).

EA rosetting and phagocytosis

The binding of immune complexes of different isotypes to Fc{gamma}RI and Fc{gamma}RII was determined using monoclonal anti-TNP Abs of known isotype incubated with TNP-coated sheep erythrocytes (EA) as described (20). In competition assays, (49-11.1) mIgG2a or (49-14.1) mIgG1 were added to the cell monolayer at 1 mg/ml and incubated for 10 min at 37°C before adding IgG3-EA.

Phagocytosis assays using BMM were performed the same as for rosetting; however, the cell monolayer was cultured at 37°C for 1 h after the addition of EA. Unbound erythrocytes were washed away before hypotonic shock of uningested EA (1 min incubation with 1 mM NaCl, pH 2.5), and the cell monolayer was washed and then fixed with 0.05% glutaraldehyde.

IgG isotype competition assays

The binding of radiolabeled monomeric IgG2a (7-20.6/3) to mouse Fc{gamma}RI-transfected CHO-K1 cells (1N3-2) was competed with various concentrations of unlabeled mouse IgG1 (UM1), IgG2a (UM2a), IgG2b (49.2), and IgG3 (UM3) and was determined as described (22). The ID50 value was determined to be the concentration of IgG at which half of the maximum level of radiolabeled IgG2a remained bound.


   Results and Discussion
Top
 Abstract
 Introduction
 Materials and Methods
 Results and Discussion
References
 
The binding of mouse IgG3 and other IgG isotypes to mouse Fc receptors was tested initially by transfection experiments. Mouse IgG3 immune complexes (IgG3-coated sheep erythrocytes (IgG3-EA)) were clearly able to bind to COS cells transfected with mouse Fc{gamma}RI cDNA (see Fig. 1Goa). This interaction had not been previously described. As expected, Fc{gamma}RI bound mIgG2a but not mIgG1 (Fig. 1Go, b and c). The observed IgG3-EA binding to mouse Fc{gamma}RI was specific, as it was inhibited by the prior addition of monomeric mouse IgG2a (Fig. 1God) but not by mouse IgG1 (Fig. 1Goe). These data demonstrated that mouse IgG2a and IgG3 isotypes competed for the same binding site on Fc{gamma}RI. In contrast, Fc{gamma}RII-transfected cells were unable to bind the IgG3 complexes (Fig. 1Gof), but did bind mIgG2a and mIgG1 complexes as expected (Fig. 1Go, g and h) (20). COS cells transfected with the expression vector alone did not bind IgG1, IgG2a, or IgG3-EA (data not shown).



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  		FIGURE 1. Mouse Fc{gamma}RI, and not Fc{gamma}RII, or Fc{gamma}RIII binds complexed mouse IgG3. Specificity of Fc{gamma}RI for IgG subclasses was tested by direct binding of immune complexes to COS cells transfected with cDNA encoding either Fc{gamma}RI (a–e) or Fc{gamma}RII (f–h). Function was tested by phagocytosis assays using macrophages derived from either Fc{gamma}RI-deficient mice (i, j) or normal littermates (k, l). IgG-sensitized EA were added to cell monolayers: mIgG3-EA (a, d, e, f, i, k); IgG2a-EA (b, g); and mIgG1-EA (c, h, j, l). Specificity of the binding of IgG3-EA to Fc{gamma}RI was confirmed by competition of IgG3-EA with either monomeric mIgG2a (d) or mIgG1 (e).

 
To demonstrate that the IgG3:Fc{gamma}RI interaction initiated phagocyte function, macrophages from either Fc{gamma}RI-deficient mice (-/-) (Fig. 1Go, i and j) or normal littermates (+/+) (Fig. 1Go, k and l) were used in assays of phagocytosis of immune complexes. Fc{gamma}RI-/- macrophages did not bind or ingest IgG3-EA (Fig. 1Goi), whereas phagocytosis of IgG1-EA (Fig. 1Goj) by Fc{gamma}RI-/- macrophages was extensive, demonstrating that the low affinity receptors expressed by macrophages, Fc{gamma}RII and Fc{gamma}RIII, were functional.

In contrast, macrophages expressing Fc{gamma}RI (+/+) readily phagocytosed IgG3-EA (Fig. 1Gok) as well as IgG1-EA (Fig. 1Gol). These data clearly demonstrated that the receptor for IgG3 expressed by macrophages was Fc{gamma}RI.

Fc{gamma}RI is able to bind both complexed IgG3 and monomeric IgG2a. The binding of monomeric IgG3 by Fc{gamma}RI was investigated using immunofluorescence. In immunofluorescence assays, there was little or no binding of monomeric mouse IgG3 to mouse Fc{gamma}RI using two different monoclonal IgG3 Abs, whereas monomeric IgG2a bound detectably (Fig. 2Goa). Clearly, mouse Fc{gamma}RI has a lower affinity for mouse IgG3 than for mouse IgG2a.



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  		FIGURE 2. Mouse Fc{gamma}RI binds monomeric mouse IgG3 with a lower affinity than IgG2a. a, FACS analysis of the binding of monomeric IgG (gray histogram) by transfected CHO cells expressing mouse Fc{gamma}RI (1N3-2). Two distinct IgG3 Abs, 5119-4 and 49-31.1, were used in addition to the positive control IgG2a Ab (UM2a). Nonspecific binding of anti-mouse Ig-FITC (F(ab')2 fragments) is shown as white histograms. b, In separate competition experiments, the inhibition of mouse IgG2a binding by monomeric IgG isotypes was performed. The inhibition of radiolabeled IgG2a (7-20.6/3) binding to mouse Fc{gamma}RI on 1N3-2 cells by mouse IgG1 (UM1) (open square), IgG2a (UM2a) (open circle), IgG2b (49.2) (closed triangle), or IgG3 (UM3) (closed circle) was determined. The data are expressed as amount of I125-labeled IgG2a bound (ng) against the concentration of competitor added (µg/ml).

 
To determine the approximate affinity of mouse Fc{gamma}RI for IgG3, a competition assay was performed. (Fig. 2Gob). Monomeric IgG3 inhibited the binding of radiolabeled mouse IgG2a at high concentrations (ID50 {approx}20 µg/ml or 1.4 x 10-7 M). As expected, cold IgG2a inhibited radiolabeled IgG2a binding and gave an ID50 value that correlated with the known affinity of this receptor for IgG2a (i.e., ID50 {approx}4 µg/ml or 2.5 x 10-8 M). In contrast, mouse IgG1 or IgG2b, at concentrations up to 45 µg/ml, were unable to inhibit the binding of IgG2a by Fc{gamma}RI, confirming that these isotypes bind poorly, if at all. This experiment confirmed that both IgG3 and IgG2a compete for the same binding site and revealed that the difference in receptor affinity for IgG2a over IgG3 is approximately fivefold.

Although Fc{gamma}RI has a moderate affinity for monomeric IgG3, the IgG3:Fc{gamma}RI interaction would be biologically significant, as complexes of IgG3, would bind to Fc{gamma}RI and induce cellular effector functions. Moreover, the approximate concentration of IgG3 in mouse serum is {approx}100 to 200 µg/ml (23), a concentration range in which Fc{gamma}RI would interact (see Fig. 2Gob).

The higher affinity of Fc{gamma}RI for IgG2a will influence the transition from a T-independent response to a maturing Th-1-type response, wherein high quantities of affinity-matured IgG2a are produced (24). The IgG2a would have a competitive affinity advantage for receptor over IgG3 of at least fivefold. Thus, in a Th-1-type response, even at low concentrations of IgG2a, the affinity maturation of IgG2a Abs leading to higher affinity for Ag, combined with a higher affinity of this subclass for Fc{gamma}RI, provides a more effective Ab for Ag clearance.

The widely held belief that mouse Fc{gamma}RI bound only IgG2a, the predominant isotype associated with Th1 type responses, led investigators to believe that mouse Fc{gamma}RI played a role in providing effector mechanisms only after T cells had been stimulated. By binding a T cell-independent Ab, Fc{gamma}RI provides a cellular effector arm for T-independent immunity and participates in the developing phases of adaptive immunity. The uptake of immune complexes via IgG3 and Fc{gamma}RI by phagocytic cells would ultimately lead to a wide range of Fc{gamma}RI-dependent responses, including Ag presentation to naive CD4+ T cells. Indeed, Fc{gamma}RI has been shown to have a major role in uptake of Ag, as immune complexes, for presentation (25). Our observations, therefore, add significantly to the role of Fc{gamma}RI; from merely responding to products of a Th-1-type response, to including an active role at the interface between the innate and the developing adaptive immune responses. Fc{gamma}RI would act together with a variety of other surface receptors in early events in immunity, including the mannose receptor and complement receptors (26, 27).

Finally, the data presented in this paper provide further insight into the pathogenic nature of IgG3 Abs. In terms of the physiologic role of the Ab, mouse IgG3 has a propensity to self-aggregate i.e., to spontaneously form small complexes and cryoglobulins (5, 6), and it is the principal Ab isotype found in glomeruli of mice with lupus nephritis (12). The role IgG3 and Fc{gamma}RI may play in tissue damage needs further investigation; however, the cross-linking of Fc{gamma}RI can lead to the release of many tissue-damaging inflammatory mediators (28). Thus, the IgG3:Fc{gamma}RI interaction implies a significant role for Fc{gamma}RI in tissue destruction by inflammatory cells in the absence of T cell help.


   Acknowledgments
 
The authors thank Dr. Bruce Loveland for useful suggestions.


   Footnotes
 
1 Address correspondence and reprint requests to Dr. P. Mark Hogarth, Kronheimer Building, The Austin Research Institute, Studley Road, Heidelberg VIC 3084, Australia. E-mail address: Back

2 Abbreviations used in this paper: TNP, trinitrophenyl; EA, erythrocyte coated with antibody; ID50, 50% inhibiting dose; BMM, bone marrow derived macrophages. Back

Received for publication September 17, 1997. Accepted for publication October 24, 1997.


   References
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 Materials and Methods
 Results and Discussion
 References
 

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Mast Cells Induce Autoantibody-Mediated Vasculitis Syndrome Through Tumor Necrosis Factor Production Upon Triggering Fcgamma Receptors
Blood, December 1, 1999; 94(11): 3855 - 3863.
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S. Wernersson, M. C. I. Karlsson, J. Dahlstrom, R. Mattsson, J. S. Verbeek, and B. Heyman
IgG-Mediated Enhancement of Antibody Responses Is Low in Fc Receptor {gamma} Chain-Deficient Mice and Increased in Fc{gamma}RII-Deficient Mice
J. Immunol., July 15, 1999; 163(2): 618 - 622.
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M. C. I. Karlsson, S. Wernersson, T. Diaz de Stahl, S. Gustavsson, and B. Heyman
Efficient IgG-mediated suppression of primary antibody responses in Fcgamma receptor-deficient mice
PNAS, March 2, 1999; 96(5): 2244 - 2249.
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T. Yuasa, S. Kubo, T. Yoshino, A. Ujike, K. Matsumura, M. Ono, J. V. Ravetch, and T. Takai
Deletion of Fcgamma Receptor IIB Renders H-2b Mice Susceptible to Collagen-induced Arthritis
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D. Meyer, C. Schiller, J. Westermann, S. Izui, W. L. W. Hazenbos, J. S. Verbeek, R. E. Schmidt, and J. E. Gessner
Fcgamma RIII (CD16)-Deficient Mice Show IgG Isotype-Dependent Protection to Experimental Autoimmune Hemolytic Anemia
Blood, December 1, 1998; 92(11): 3997 - 4002.
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W. L. W. Hazenbos, I. A. F. M. Heijnen, D. Meyer, F. M. A. Hofhuis, C. Renardel de Lavalette, R. E. Schmidt, P. J. A. Capel, J. G. J. van de Winkel, J. E. Gessner, T. K. van den Berg, et al.
Murine IgG1 Complexes Trigger Immune Effector Functions Predominantly via Fc{gamma}RIII (CD16)
J. Immunol., September 15, 1998; 161(6): 3026 - 3032.
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H. L. Rotman, T. M. Daly, R. Clynes, and C. A. Long
Fc Receptors Are Not Required for Antibody-Mediated Protection Against Lethal Malaria Challenge in a Mouse Model
J. Immunol., August 15, 1998; 161(4): 1908 - 1912.
[Abstract] [Full Text] [PDF]

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