Abstract
The ninth component of complement (C9) has a marked propensity to polymerize. C9 polymers [poly(C9)] formed spontaneously in Veronal-buffered saline upon incubation of purified C9 for 64 hr at 37 degrees C or within 2 hr at 46--56 degrees C. Poly(C9) formed at 37 degrees C was visualized by electron microscopy as a tubular structure with an internal diameter of 110 A and a length of 160 A. Its ultrastructure suggested a dodecameric composition and resembled that of the membrane attack complex of complement. The wider end of the tubular structure was formed by an approximately 30-A-thick torus with inner and outer diameters of 110 A and 220 A, respectively. Because the dimensions of C9 within poly(C9) were 160 x 55 A (maximal) and 20 A (minimal) and because monomeric C9 has dimensions of approximately 80 x 55 A, it is proposed that monomeric C9 unfolds during polymerization into tubules. Polymerization also occurred upon treatment of C9 for 1 hr at 37 degrees C with 0.6 M guanidine . HCl, 0.1 M octyl glucoside, or 1.5% sodium deoxycholate. Guanidine . HCl-induced C9 polymers consisted of elongated highly curved strands 55--80 A wide, suggesting that these polymers were formed by globular C9 that had not unfolded.
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- Bhakdi S., Tranum-Jensen J. Evidence for a two-domain structure of the terminal membrane C5b-9 complex of human complement. Proc Natl Acad Sci U S A. 1979 Nov;76(11):5872–5876. doi: 10.1073/pnas.76.11.5872. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bhakdi S., Tranum-Jensen J. Molecular weight of the membrane C5b-9 complex of human complement: characterization of the terminal complex as a C5b-9 monomer. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1818–1822. doi: 10.1073/pnas.78.3.1818. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Biesecker G., Müller-Eberhard H. J. The ninth component of human complement: purification and physicochemical characterization. J Immunol. 1980 Mar;124(3):1291–1296. [PubMed] [Google Scholar]
- Biesecker G., Podack E. R., Halverson C. A., Müller-Eberhard H. J. C5b-9 dimer: isolation from complement lysed cells and ultrastructural identification with complement-dependent membrane lesions. J Exp Med. 1979 Feb 1;149(2):448–458. doi: 10.1084/jem.149.2.448. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Boyle M. D., Borsos T. Studies on the terminal stages of immune hemolysis. V. Evidence that not all complement-produced transmembrane channels are equal. J Immunol. 1979 Jul;123(1):71–76. [PubMed] [Google Scholar]
- Boyle M. D., Gee A. P., Borsos T. Studies on the terminal stages of immune hemolysis. VI. Osmotic blockers of differing Stokes' radii detect complement-induced transmembrane channels of differing size. J Immunol. 1979 Jul;123(1):77–82. [PubMed] [Google Scholar]
- Dourmashkin R. R. The structural events associated with the attachment of complement components to cell membranes in reactive lysis. Immunology. 1978 Aug;35(2):205–212. [PMC free article] [PubMed] [Google Scholar]
- Esser A. F., Kolb W. P., Podack E. R., Müller-Eberhard H. J. Molecular reorganization of lipid bilayers by complement: a possible mechanism for membranolysis. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1410–1414. doi: 10.1073/pnas.76.3.1410. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Giavedoni E. B., Chow Y. M., Dalmasso A. P. The functional size of the primary complement lesion in resealed erythrocyte membrane ghosts. J Immunol. 1979 Jan;122(1):240–245. [PubMed] [Google Scholar]
- Hadding U., Müller-Eberhard H. J. The ninth component of human complement: isolation, description and mode of action. Immunology. 1969 Jun;16(6):719–735. [PMC free article] [PubMed] [Google Scholar]
- Hammer C. H., Wirtz G. H., Renfer L., Gresham H. D., Tack B. F. Large scale isolation of functionally active components of the human complement system. J Biol Chem. 1981 Apr 25;256(8):3995–4006. [PubMed] [Google Scholar]
- Hu V. W., Esser A. F., Podack E. R., Wisnieski B. J. The membrane attack mechanism of complement: photolabeling reveals insertion of terminal proteins into target membrane. J Immunol. 1981 Jul;127(1):380–386. [PubMed] [Google Scholar]
- Klob W. P., Müller-Eberhard H. J. The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8). J Exp Med. 1976 May 1;143(5):1131–1139. doi: 10.1084/jem.143.5.1131. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kolb W. P., Haxby J. A., Arroyave C. M., Müller-Eberhard H. J. Molecular analysis of the membrane attack mechanism of complement. J Exp Med. 1972 Mar 1;135(3):549–566. doi: 10.1084/jem.135.3.549. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kolb W. P., Müller-Eberhard H. J. Mode of action of human C9: adsorption of multiple C9 molecules to cell-bound C8. J Immunol. 1974 Aug;113(2):479–488. [PubMed] [Google Scholar]
- Mayer M. M. Mechanism of cytolysis by complement. Proc Natl Acad Sci U S A. 1972 Oct;69(10):2954–2958. doi: 10.1073/pnas.69.10.2954. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Michaels D. W., Abramovitz A. S., Hammer C. H., Mayer M. M. Increased ion permeability of planar lipid bilayer membranes after treatment with the C5b-9 cytolytic attack mechanism of complement. Proc Natl Acad Sci U S A. 1976 Aug;73(8):2852–2856. doi: 10.1073/pnas.73.8.2852. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Monahan J. B., Sodetz J. M. Binding of the eighth component of human complement to the soluble cytolytic complex is mediated by its beta subunit. J Biol Chem. 1980 Nov 25;255(22):10579–10582. [PubMed] [Google Scholar]
- Okada M., Boyle M. D., Borsos T. Evidence for a temperature-dependent and temperature-independent pathway in the generation of complement-mediated transmembrane channels. Biochem Biophys Res Commun. 1980 May 14;94(1):406–412. doi: 10.1016/s0006-291x(80)80235-x. [DOI] [PubMed] [Google Scholar]
- Podack E. R., Biesecker G., Kolb W. P., Müller-Eberhard H. J. The C5b-6 complex: reaction with C7, C8, C9. J Immunol. 1978 Aug;121(2):484–490. [PubMed] [Google Scholar]
- Podack E. R., Biesecker G., Müller-Eberhard H. J. Membrane attack complex of complement: generation of high-affinity phospholipid binding sites by fusion of five hydrophilic plasma proteins. Proc Natl Acad Sci U S A. 1979 Feb;76(2):897–901. doi: 10.1073/pnas.76.2.897. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Podack E. R., Esser A. F., Biesecker G., Müller-Eberhard H. J. Membrane attack complex of complement: a structural analysis of its assembly. J Exp Med. 1980 Feb 1;151(2):301–313. doi: 10.1084/jem.151.2.301. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Podack E. R., Kolb W. P., Esser A. F., Müller-Eberhard H. J. Structural similarities between C6 and C7 of human complement. J Immunol. 1979 Sep;123(3):1071–1077. [PubMed] [Google Scholar]
- Podack E. R., Müller-Eberhard H. J. Membrane attack complex of complement. Evidence for its dimeric structure based on hybrid formation. J Biol Chem. 1981 Apr 10;256(7):3145–3148. [PubMed] [Google Scholar]
- Podack E. R., Stoffel W., Esser A. F., Müller-Eberhard H. J. Membrane attack complex of complement: distribution of subunits between the hydrocarbon phase of target membranes and water. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4544–4548. doi: 10.1073/pnas.78.7.4544. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ramm L. E., Mayer M. M. Life-span and size of the trans-membrane channel formed by large doses of complement. J Immunol. 1980 May;124(5):2281–2287. [PubMed] [Google Scholar]
- Rommel F. A., Mayer M. M. Studies of guinea pig complement component C9: reaction kinetics and evidence that lysis of EAC1-8 results from a single membrane lesion caused by one molecule of C9. J Immunol. 1973 Mar;110(3):637–647. [PubMed] [Google Scholar]
- Seegan G. W., Smith C. A., Schumaker V. N. Changes in quaternary structure of IgG upon reduction of the interheavy-chain disulfide bond. Proc Natl Acad Sci U S A. 1979 Feb;76(2):907–911. doi: 10.1073/pnas.76.2.907. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Simone C. B., Henkart P. Permeability changes induced in erthrocyte ghost targets by antibody-dependent cytotoxic effector cells: evidence for membrane pores. J Immunol. 1980 Feb;124(2):954–963. [PubMed] [Google Scholar]
- Sims P. J., Lauf P. K. Analysis of solute diffusion across the C5b-9 membrane lesion of complement: evidence that individual C5b-9 complexes do not function as discrete, uniform pores. J Immunol. 1980 Dec;125(6):2617–2625. [PubMed] [Google Scholar]
- Sims P. J., Lauf P. K. Steady-state analysis of tracer exchange across the C5b-9 complement lesion in a biological membrane. Proc Natl Acad Sci U S A. 1978 Nov;75(11):5669–5673. doi: 10.1073/pnas.75.11.5669. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Steckel E. W., York R. G., Monahan J. B., Sodetz J. M. The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure. J Biol Chem. 1980 Dec 25;255(24):11997–12005. [PubMed] [Google Scholar]
- Stolfi R. L. Immune lytic transformation: a state of irreversible damage generated as a result of the reaction of the eighth component in the guinea pig complement system. J Immunol. 1968 Jan;100(1):46–54. [PubMed] [Google Scholar]
- Tranum-Jensen J., Bhakdi S., Bhakdi-Lehnen B., Bjerrum O. J., Speth V. Complement lysis: the ultrastructure and orientation of the C5b-9 complex on target sheep erythrocyte membranes. Scand J Immunol. 1978;7(1):45–46. doi: 10.1111/j.1365-3083.1978.tb00425.x. [DOI] [PubMed] [Google Scholar]
- Tschopp J., Podack E. R. Membranolysis by the ninth component of human complement. Biochem Biophys Res Commun. 1981 Jun 16;100(3):1409–1414. doi: 10.1016/0006-291x(81)91981-1. [DOI] [PubMed] [Google Scholar]
- Ware C. F., Wetsel R. A., Kolb W. P. Physicochemical characterization of fluid phase (SC5b-9) and membrane derived (MC5b-9) attack complexes of human complement purified by immunoadsorbent affinity chromatography or selective detergent extraction. Mol Immunol. 1981 Jun;18(6):521–531. doi: 10.1016/0161-5890(81)90130-9. [DOI] [PubMed] [Google Scholar]
- Wetsel R. A., Jones M. A., Kolb W. P. Immunoadsorbent affinity purification of the fifth component (C5) of human complement and development of a highly sensitive hemolytic assay. J Immunol Methods. 1980;35(3-4):319–335. doi: 10.1016/0022-1759(80)90258-6. [DOI] [PubMed] [Google Scholar]