Immunoglobulin G antibody bound to the C1q subcomponent of human complement exhibits segmental flexibility.
The rotational dynamics of rabbit immunoglobulin G (IgG) anti-dansyl antibodies bound to the C1q subcomponent of human complement were studied by nanosecond fluorescence spectroscopy. Deconvoluted anisotropy decays of IgG-C1q mixtures were fitted to a two-exponential expression and were corrected for the effects of unbound IgG, which was determined with an analytical ultracentrifuge. Compared with the anisotropy parameters for free IgG, the pre-exponential weighting factors and the short correlation time of the C1q-bound antibody were nearly unchanged, and the long correlation time increased by only about 45 nanoseconds. These results, together with rotational diffusion calculations, indicate that the Fab arms of the C1q-bound antibody exhibited considerable flexibility. This finding may have biological relevance because it suggests that C1q can bind to the Fc segments of IgG molecules anchored in an immune complex, even though the angles between the two Fab arms of the different antibodies may vary. The results of this study also support our earlier interpretation that both the short and long correlation times of IgG principally represent flexible motions of the Fab segments.
D000818:Animals; D003166:Complement Activating Enzymes / Q000276:immunology* / Q000378:metabolism; D015922:Complement C1q; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology* / Q000378:metabolism; D046911:Macromolecular Substances; D011817:Rabbits; D012399:Rotation; D013050:Spectrometry, Fluorescence; D014461:Ultracentrifugation
D007074:Immunoglobulin G; D046911:Macromolecular Substances; D015922:Complement C1q; D003166:Complement Activating Enzymes