Open AccessMolecular nature of the complement lesion.
Author(s) -
Sucharit Bhakdi,
Jørgen TranumJensen
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.11.5655
Subject(s) - macromolecule , lipid bilayer , biophysics , membrane , complement system , vesicle , chemistry , transmembrane protein , complement component 5 , complement membrane attack complex , complement (music) , bilayer , biochemistry , microbiology and biotechnology , biology , receptor , antibody , immunology , complementation , gene , phenotype
The principle molecular event leading to membrane perturbation by complement is the assembly of the terminal five serum complement components (C5b-C9) into a macromolecular C5b-9 complex on the target membrane [Müller-Eberhard, H.-J. (1975) Ann. Rev. Biochem. 44, 697--723]. The present communication reports on the ability of purified C5b-9 complexes isolated from target membranes to become reincorporated into artificial lipid vesicles. The data indicate that the complex is a vertically oriented, hollow, cylindrical macromolecule possessing lipid-binding regions that enable one terminus to penetrate into the lipid bilayer. A transmembrane pore appears to be created at the attachment site of the C5b-9 complex.