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Fc:Fc interactions revealed by spin-labeled IgG heterosaccharides in model immune complexes
Authors:A Kusumi  J L Winkelhake
Institution:1. Microphotonic Center, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226 USA;2. Department of Biophysics, Faculty of Science, Kyoto University, Kyoto 606, Japan;3. CETUS Corporation, 1400 Fifty-third Street, Emeryville, CA 94608 USA;1. Department of Psychiatry, Peking University People''s Hospital, China;2. Sleep Medicine Department, Sanya Central Hospital, The Third People''s Hospital of Hainan Province, China;3. School of Nursing, Peking University, China;4. Department of Respiratory and Critical Care Medicine, Peking University People''s Hospital, China;1. Department of Clinical Microbiology, Infectious Diseases, Umeå University, Sweden;2. Department of Medical Sciences, Section of Infectious Diseases, Uppsala University, Sweden;3. Department of Clinical Sciences, Division of Infection Medicine, Lund University, Sweden;4. School of Medical Sciences, Örebro University, Örebro, Sweden;5. Department of Infectious Diseases, Örebro University Hospital, Örebro, Sweden;6. Department of Infectious Diseases, Skåne University Hospital, Malmö, Region Skåne, Sweden;7. Department of Infectious Diseases, Sahlgrenska University Hospital, Gothenburg, Sweden;8. Department of Medicine, Solna, Division of Infectious Diseases, Karolinska Institutet, Sweden;9. Academic Specialist Centre, Stockholm County Health Care Services, Region Stockholm, Sweden;1. Department of Medicine, Stanford University School of Medicine, Stanford, CA 94305, USA;2. Proteomics Facility, Institute of Biotechnology, Cornell University, Ithaca, NY 14853, USA;3. The Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA;4. Department of Immunology and Rheumatology, Stanford University, Stanford, CA 94305, USA;5. Viral Pathogenesis and Evolution Section, Laboratory of Infectious Diseases, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA;6. Department of Biomedical Data Science, Stanford University, Stanford, CA 94305, USA;7. University of Massachusetts Medical School, Worcester, MA, USA;8. Department of Microbiology and Immunology, Stanford University, Stanford, CA 94305, USA;9. Chan Zuckerberg Biohub, San Francisco, CA 94518, USA;1. Laboratorio de Investigaciones Infectológicas y Biología Molecular, Unidad de Infectología, Departamento de Medicina, Hospital de Niños Dr. Ricardo Gutiérrez, Buenos Aires 1425, Argentina;2. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires 1425, Argentina;1. Department of Chemistry, Indiana University, Bloomington, Indiana;2. Department of Surgery, School of Medicine, University of Louisville, Louisville, Kentucky
Abstract:Dynamic properties of spin-labelled heterosaccharides in the Fc-region of murine monoclonal antihapten immunoglobulin G were studied in model immune complexes (IC) as a function of the IC size. Model IC dimers, trimers and oligomers were formed using bivalent photoaffinity antigens. The ESR spectrum exhibits two components. The rotational correlation time of the less-immobilized species is shorter than 10(-10) sec, and that of the more-immobilized component is in the order to 10(-9) approximately 10(-8) sec depending on the IC size. Fraction of the more-immobilized spin labels increases, and the mobility of this component decreases with increase in IC size (i.e., mobility: monomers approximately equal to dimers greater than trimers much greater than immune-complex precipitates). These data strongly suggest the existence of Fc:Fc interactions in IC, and provide the basis for a model in which such interactions underlie the initial mechanism by which the information of antigen binding to Fab region is transferred into organized Fc:Fc association structure for IgG effector activities.
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