Immunoglobulin Structure and Function as Revealed by Electron MicroscopyRoux K.H.
Department of Biological Science, Florida State University, Tallahassee, Fla., USA
Do you have an account?
- Rent for 48h to view
- Buy Cloud Access for unlimited viewing via different devices
- Synchronizing in the ReadCube Cloud
- Printing and saving restrictions apply
Rental: USD 8.50
Cloud: USD 20.00
Electron–microscopic (EM) analysis preceded crystallographic analysis [
- Huber R, Deisenhofer J, Colman PM, Matsushima M: Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature 1976;264:415–420.
- Silverton EW, Navia MA, Davies DR: Three–dimensional structure of an intact human immunoglobulin. Proc Natl Acad Sci USA 1977; 74:5140–5144.
- Seegan GW, Smith CA, Schumaker VN: Changes in quaternary structure of IgG upon reduction of the interheavy–chain disulfide bond. Proc Natl Acad Sci USA 1979;76:907– 911.
- Roux KH: Immunoelectron microscopy of idiotype–anti–idiotype complexes. Methods Enzymol 1989;178:130–144.
- Roux KH: Negative stain immunoelectron microscopic analysis of small macromolecules of immunologic significance. Methods 1996;10: 247.
- Lansdorp PM, Aalberse RC, Bos R, Schutter WG, Van Bruggen EFJ: Cyclic tetramolecular complexes of monoclonal antibodies: A new type of cross–linking reagent. Eur J Immunol 1986;16:679–683.
- Uzgiris EE, Kornberg RD: Two–dimensional crystallization technique for imaging macromolecules, with application to antigen–antibody–complement complexes. Nature 1983; 301:125–129.
- Uzgiris EE: Antibody crystallization on phospholipid films: Dynamics and the effects of antibody conformation. J Cell Biochem 1985;29: 239–251.
- Uzgiris EE: Self–organization of IgE immunoglobulins on phospholipid films. Biochem J 1987;242:293–296.
- Unwin PN, Henderson R: Molecular structure determination by electron microscopy of unstained crystalline specimens. J Mol Biol 1975;94:425–440.
- Jentoft JE, Bolinger L, Ainslie GR, Tandler B: Forms of a self associating autoantibody complex between a monoclonal human IgG1 and human serum albumin. Mol Immunol 1987;24: 163–169.
- Tesche B, Schmiady H: Comparative electron microscopic studies of single biomolecules negatively stained and freeze–dried metal–shadowed. Ultramicroscopy 1985;16:423–435.
- Ryazantsev SN, Abramov VM, Azv’yalov VP, Vasiliev VD: Electron microscopy study of human myeloma immunoglobulin G1. FEBS Lett 1990;275:221–225.
- Baccala R, Builbert B, Labrousse H, Avrameas S, Gounon P: Visualization of natural autoantibody polyreactivity by rotary metal–shadowing electron microscopy. Res Immunol 1991; 142:299–312.
- Dubochet J, Adrian M, Chang J–J, Homo J–C, Lepault J, McDowall AW, Schultz P: Cryo–electron microscopy of vitrified specimens. Q Rev Biophys 1988;21:129–228.
Frank J: Three–Dimensional Electron Microscopy of Macromolecular Assemblies. New York, Academic Press, 1996, pp 1–341.
- Wang G, Porta C, Chen Z, Baker TS, Johnson JE: Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X–ray crystallography. Nature 1992;355:275–278.
- Smith TJ, Olson NH, Cheng RH, Liu H, Chase ES, Lee WM, Leippe DM, Mosser AG, Rueckert RR, Baker TS: Structure of human rhinovirus complexed with Fab fragments from a neutralizing antibody. J Virology 1993;67: 1148–1158.
- Hewat EA, Verdaguer N, Fita I, Blakemore W, Brookes S, King A, Newman J, Domingo E, Mateu MG, Stuart DI: Structure of the complex of an Fab fragment of a neutralizing antibody with foot–and–mouth disease virus: Positioning of a highly mobile antigenic loop. EMBO J 1997;16:1492–1500.
- Hewat EA, Marlovits TC, Blaas D: Structure of a neutralizing antibody bound monovalently to human rhinovirus 2. J Virol 1998;72: 4396–4402.
- Davies J, Roberts CJ, Dawkes AC, Sefton J, Edwards JC, Glasbey TO, Haymes AG, Davies MC, Jackson DE, Lomas M, Shakesheff KM, Tendler SJB, Wilkins MJ, Williams PM: Use of scanning probe microscopy and surface plasmon resonance as analytical tools in the study of antibody–coated microtiter wells. Langmuir 1994;10:2654–2661.
Roberts CJ, Williams PM, Davies J, Dawkes AC, Sefton J, Edwards JC, Haymes AG, Bestwic C, Davies MC, Tendler SJB: Real–space differentiation of IgG and IgM antibodies deposited on microtiter wells by scanning force microscopy. Langmuir 1995;11:1822–1826.
- Weisenhorn AL, Gaub HE, Hansma HG, Sinsheimer RL, Kelderman GL, Kansma PK: Imaging single–stranded DNA, antigen–antibody reaction and polymerized langmuir–blodgett films with an atomic force microscope. Scanning Microscopy 1990;4:511–516.
- Quist AP, Bergman AA, Reimann CT, Oscarsson SO, Sundqvist BUR: Imaging of single antigens, antibodies, and specific immunocomplex formation by scanning force microscopy. Scan Microsc 1995;9:395–400.
- Zhang Y, Sheng S, Shao Z: Imaging biological structures with the cryo atomic force microscope. Biophys J 1996;71:2168–2176.
Feinstein A, Rowe AJ: Molecular mechanism of formation of an antigen–antibody complex. Nature 1965;205:147–149.
- Valentine RC, Green NM: Electron microscopy of an antibody–hapten complex. J Mol Biol 1967;27:615–617.
Pumphrey R: Computer models of the human immunoglobulins. Shape and segmental flexibility. Immunol Today 1986:174–178
- Phillips ML, Tao M–H, Morrison SL, Schumaker VN: Human/mouse chimeric monoclonal antibodies with human IgG1, IgG2, IgG3 and IgG4 constant domains: Electron microscopic and hydrodynamic characterization. Molec Immunol 1994;31:1201–1210.
- Roux KH, Strelets L, Michaelsen TE: Flexibility of human IgG subclasses. J Immunol 1997; 159:3372–3382.
- Chesebro B, Bloth B, Svehag SE: The ultrastructure of normal and pathological IgM. J Exp Med 1968;127:399–410.
- Parkhouse RME, Askonas BA, Dourmashkin RR: Electron microscopic studies of mouse immunoglobulin M: Structure and reconstitution following reduction. Immunology 1970; 18:575–584.
- Feinstein A, Munn EA, Richardson NE: The three–dimensional conformation of gamma M and gamma A globulin molecules. Ann NY Acad Sci 1971;190:104–121.
- Garrido J, Ioannes A: Electron microscopy of the natural IgM–like hemagglutinin of the ratfish (Callorhynchus callorhynchus). Dev Comp Immunol 1981;5:691–696.
- Johnston WH Jr, Acton RT, Weineimer PF, Niedermeier W, Evans EE, Shelton E, Bennett JC: Isolation and physico–chemical characterization of the ‘IgM–like’ immunoglobulin from the stingray Dasyatis americana. J Immunol 1971;107:782–793.
- Hadji–Azimi I, Michea–Hamzehpour M: Xenopus laevis 19S immunoglobulin: Ultrastructure and J chain isolation. Immunology 1976;30: 587–591.
- Acton RT, Weinheimer PF, Hall SJ, Nieermeier W, Shelton E, Bennett JC: Tetrameric immune macroglobulins in three orders of bony fishes. Proc Natl Acad Sci USA 1971;68:107–111.
- Shelton E, Smith M: The ultrastructure of carp (Cyprinus carpio) immunoglobulin: A tetrameric macroglobulin. J Mol Biol 1970;54: 615–617.
- Wilhelm P, Pilz I, Palm W, Bauer K: Small–angle X–ray studies of a human immunoglobulin M. Eur J Biochem 1978;84:457–463.
- Poon PH, Phillips ML, Schumaker VN: Immunoglobulin M possesses two binding sites for complement subcomponent C1q, and soluble 1:1 and 2:1 complexes are formed in solution at reduced ionic strength. J Biol Chem 1985;260:9357–9365.
- Davis AC, Roux KH, Pursey J, Shulman MJ: Intermolecular disulfide bonding in IgM: Effects of replacing cystein residues in the mu heavy chain. EMBO J 1989;8:2519–2526.
- Feinstein A, Richardson N, Taussig MJ: Immunoglobulin flexibility in complement activation. Immunol Today 1986;7:169.
- Perkins SJ, Nealis AS, Sutton BJ, Feinstein A: Solution structure of human and mouse immunoglobulin M by synchroton x–ray scattering and molecular graphics modelling: A possible mechanism for complement activation. J Mol Biol 1991;221:1345–1366.
- Cattaneo A, Neuberger MS: Polymeric immunoglobulin M is secreted by transfectants of non–lymphoid cells in the absence of immunoglobulin J chain. EMBO J 1987;6:2753– 2758.
- Davis AC, Roux KH, Shulman MJ: On the structure of polymeric IgM. Eur J Immunol 1988;18:1001–1008.
- Dourmashkin RB, Virella G, Parkhouse RM: Electron microscopy of human and mouse myeloma serum IgA. J Mol Biol 1971;56:207– 208.
- Roux KH, Greenberg AS, Greene L, Strelets L, Avila D, McKinney EC, Flajnik MF: Structural analysis of the nurse shark (new) antigen receptor (NAR): Molecular convergence of NAR and unusual mammalian immunoglobulins. Proc Natl Acad Sci USA 1998;95:11804– 11809.
- Nezlin R: Internal movement in immunoglobulin molecules. Adv Immunol 1990;48:1–40.
- Wrigley NG, Brown EB, Shehel JJ: Electron microscopic evidence for the axial rotation and inter–domain flexibility of the Fab regions of immunoglobulin G. J Mol Biol 1983;169:771– 774.
Lamy J, Lamy J, Billiald P, Sizaret P–Y, Cave G, Frank J, Motta G: Approach to the direct intramolecular localization of antigenic determinants in Androctonus australis hemocyanin with monoclonal antibodies by molecular immunoelectron microscopy. Biochemistry 1985;24:5532:5542.
- Wade RH, Taveau JC, Lamy JN: Concerning the axial rotational flexibility of the Fab regions of immunoglobulin G. J Mol Biol 1989; 206:349–356.
- Roux KH, Metzger DW: Immunoelectron microscopic localization of idiotypes and allotypes on immunoglobulin molecules. J Immunol 1982;129:2548–2553.
- Roux KH: Direct demonstration of multiple VH allotypes on rabbit Ig molecules: Allotype characteristics and Fab arm rotational flexibility revealed by immunoelectron microscopy. Eur J Immunol 1984;14:459–464.
- Sheriff S, Silverton EW, Padlan EA, Cohen GH, Smith–Gill SJ, Fenzel BC, Davies DR: Three–dimensional structure of an antibody–antigen complex. Proc Natl Acad Sci USA 1987;84:8075–8079.
Prasad L, Vandonselaar M, Lee JS, Delbaere L: Structure determination of a monoclonal Fab fragment specific for histidine–containing protein of the phosphoenolypyruvate: Sugar phosphotransferase system of Escherichia coli. J Biol Chem 1988;15:2571–2574.
- Roux KH, Metzger DW, Kazdin DS, Horng WJ: Induced latent allotypes within rabbit anti–crossreactive idiotype reagents: Direct immunoelectron microscopic evidence. Eur J Immunol 1984;14:910–915.
- Roux KH, McCormack WT, Dhanarajan P: A reevaluation of rabbit anti–allotype antibody for the presence of cross–reactive idiotypes. I. A species–specific idiotope on rabbit anti–a1 antibody is recognized by guinea pig anti–IdX antibody. J Immunol 1985;135:1961–1966.
- McClain BR, Roux KH: Mouse monoclonal antibody bearing a VH framework region determinant similar to a rabbit Vha1 allotype. Immunology 1987;61:397–402.
- Mage RG, Bernstein KE, McCartney Francis N, Alexander CB, YoungCooper GO, Padlan EA, Cohen GH: The structural and genetic basis for expression of normal and latent VHa allotypes of the rabbit. Mol Immunol 1984; 21:1067–1081.
- Roux KH, Monafo WJ, Davie JM, Greenspan NS: Construction of an extended three–dimensional idiotope map by electron microscopic analysis of idiotope–anti–idiotope complexes. Proc Natl Acad Sci USA 1987;84:4984–4988.
- Greenspan NS, Davie JM: Serologic and topographic characterization of idiotopes on murine monoclonal anti–streptococcal group A carbohydrate antibodies. J Immunol 1985;134: 1065–1072.
- Murphy RM, Slayter H, Schurtenberger P, Chamberlin RA, Colton CK, Yarmush ML: Size and structure of antigen–antibody complexes: Electron microscopy and light scattering studies. Biophys J 1988;54:45–56.
- Roux KH, Greenspan NS: Monitoring the formation of soluble immune complexes composed of idiotype and anti–idiotype antibodies by electron microscopy. Mol Immunol 1994; 31:599–606.
- Phillips ML, Oi VT, Schumaker VN: Electron microscopic study of ring–shaped, bivalent hapten, bivalent antidansyl monoclonal antibody complexes with identical variable domains but IgG1, IgG2 and IgG2b constant domains. Mol Immunol 1990;27:181–190.
- Dangl JL, Wensel TG, Morrison SL, Stryer L, Herzenberg LA, Oi VT: Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. EMBO J 1988;7:1989–1994.
- Schumaker VN, Phillips ML, Hanson DC: Dynamic aspects of antibody structure. Mol Immunol 1991;28:1347–1360.
- Roux KH, Strelets L, Brekke OH, Sandlie I, Michaelsen TE: Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry. J Immunol 1998;161:4083–4090.
- Klein M, HaeffnerCavaillon N, Isenman DE, Rivat C, Navia MA, Davies DR, Dorrington KJ: Expression of biological effector functions by immunoglobulin G molecules lacking the hinge region. Proc Natl Acad Sci USA 1981; 78:524–528.
Nezlin R: The Immunoglobulins: Structure and Function. New York, Academic Press, 1998, pp 1–269.
- Roux KH, Shuford WW, Finley JW, Esselstyn J, Pankey S, Raff HV, Harris LJ: Characterization of biosynthetic IgG oligomers resulting from light chain variable domain duplication. Mol Immunol 1994;31:933–942.
- Lawrence LJ, Kortt AA, Iliades P, Tulloch PA, Hudson PJ: Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments. FEBS Lett 1998;425: 479–484.
- Gronski P, Bauer R, Bodenbender L, Boland P, Diderrich G, Harthus HP, Kanzy EJ, Kuhn K, Schmidt KH, Walter G, Wiedemann H, Zilg H, Seiler FR: On the nature of IgG dimers. II. Idiotype–anti–idiotype complexes of polyclonal and monoclonal origin: Size distribution patterns and molecular geometries. Behring Inst Mitt 1988;82:144–153.
- Roux KH, Tankersley DL: A view of the human idiotypic repertoire: electron microscopic and immunologic analyses of spontaneous idiotype–anti–idiotype dimers in pooled human IgG. J Immunol 1990;144:1387–1395.
Rudich SM, Roux KH, Winchester RJ, Mongini PKA: Anti–IgM–mediating B cell signaling: molecular analysis of ligand binding requisites for human B cell activation and tolerance. J Exp Med 1988;268:247–266.
- Wharton SA, Calder LJ, Ruigrok RWH, Skehel JJ, Steinbauer DA, Wiley DC: Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO J 1995;14:240–246.
- Moller NPH, Christiansen G: Fc–mediated immune precipitation. III. Visualization by electron microscopy. Immunology 1983;48:469.
- Hyslop NE, Dourmashkin RR, Green NM, Porter RR: The fixation of complement and the activated first component (C1) of complement by complexes formed between antibody and divalent hapten. J Exp Med 1970;131:783– 802.
- Burton DR: Is IgM–like dislocation a common feature of antibody function? Immunol Today 1986;7:165–167.
- Beavil AJ, Young RJ, Sutton BJ, Perkins SJ: Bent domain structure of recombinant human IgE–Fc in solution by X–ray and neutron scattering in conjunction with an automated curve fitting procedure. Biochemistry 1995;34: 14449–14461.
- Smith T, Olson N, Cheng R, Chase E, Baker T: Structure of a human rhinovirus–bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility. Proc Natl Acad Sci USA 1993;90:7015–7018.
Article / Publication Details
Copyright / Drug Dosage / DisclaimerCopyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher.
Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.