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The Journal of Immunology, Vol 148, Issue 11 3550-3553, Copyright © 1992 by American Association of Immunologists

ARTICLES

Surface-bound immune complexes trigger transmembrane proximity between complement receptor type 3 and the neutrophil's cortical microfilaments

MJ Zhou, H Poo, RF Todd 3d and HR Petty
Department of Biological Sciences, Wayne State University, Detroit, MI 48202.

To characterize the transmembrane associations participating in antibody-dependent binding, we have used resonance energy transfer (r.e.t.) microscopy to assess the molecular proximity of complement receptor type 3 (CR3) and Fc gamma R type II (Fc gamma RII) and type III (Fc gamma RIII) with microfilaments during neutrophil adherence to untreated surfaces, surfaces coated with BSA, surfaces coated with BSA/anti-BSA F(ab')2 complexes, or surfaces coated with BSA/anti-BSA rabbit IgG immune complexes. Receptors were labeled with fluorescein- conjugated antireceptor Fab fragments, whereas microfilaments were labeled with rhodamine-phalloidin. CR3-to-microfilament r.e.t. was dramatically increased in neutrophils adherent to IgG immune complex- coated surfaces but not untreated or control surfaces. However, the low level of r.e.t. between donor-labeled anti-Fc gamma RII Fab fragments and rhodamine-phalloidin was not affected by any condition including surface-bound immune complexes. Significant r.e.t. levels between Fc gamma RIII and microfilaments were not found under any condition. We suggest that CR3 plays an important role in tethering surface-attached immune complexes to the neutrophil's cytoskeleton.


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