Visualization of specific antibody and C1q binding to hapten-sensitized lipid vesicles.
Authors:
- N HenryNHN Henry
- J W ParceJPJ W Parce
- H M McConnellHMH M McConnell
- 1 August 1978
- journal article
- research article
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (8) , 3933-3937
Abstract
Specific IgG antibodies directed against the spin-label nitroxide group present as a lipid hapten in single-compartment lipid vesicles have been visualized by using freeze-etch electron microscopy. Individual "particles" with diameters of the order of 20 nm are identified as single IgG molecules bound to lipid hapten. No significant aggregation of these IgG molecules was observed over a period of 1 hr in a dipalmitoyl phosphatidylcholine vesicle at 22 degrees. Binding of the human complement component C1q results in the formation of large (approximately 50-100 nm) asymmetric particles having a partially resolved substructure that may arise from individual IgG molecules bound to the membranes as well as to C1q. The binding of C1q appears to result in a clustering of membrane-bound IgG molecules. Samples containing a serum factor (perhaps anti-IgG antibodies) exhibit some IgG clustering distinct from that produced by Clq.Keywords
This publication has 12 references indexed in Scilit:
- Specific antibody-dependent binding of complement component C1q to hapten-sensitized lipid vesicles.Proceedings of the National Academy of Sciences, 1978
- The Biochemistry of ComplementBiochemical Society Transactions, 1977
- Membrane-controlled depletion of complement activity by spin-label-specific IgMProceedings of the National Academy of Sciences, 1977
- Lateral hapten mobility and immunochemistry of model membranes.Proceedings of the National Academy of Sciences, 1976
- Large volume liposomes by an ether vaporization methodBiochimica et Biophysica Acta (BBA) - Biomembranes, 1976
- Antigen mobility in membranes and complement-medical immune attack.Proceedings of the National Academy of Sciences, 1975
- Chemical analysis and electron microscopy studies of human C1q prepared by different methodsEuropean Journal of Immunology, 1975
- A Simple Method for the Isolation of the Subcomponents of the First Component of Complement by Affinity ChromatographyThe Journal of Immunology, 1974
- HOMOGENEOUS RABBIT 7S ANTI-IGG WITH ANTIBODY SPECIFICITY FOR PEPTIDOGLYCANJournal of Experimental Medicine, 1973
- C1q: Rapid Purification Method for Preparation of Monospecific Antisera and for Biochemical StudiesThe Journal of Immunology, 1971