© 2003 Robert A. Freitas Jr. All Rights Reserved.

Robert A. Freitas Jr., Nanomedicine, Volume IIA: Biocompatibility, Landes Bioscience, Georgetown, TX, 2003

References 1700-1799

1700. O.B. Spiller, B.P. Morgan, F. Tufaro, D.V. Devine, “Altered expression of host-encoded complement regulators on human cytomegalovirus-infected cells,” Eur. J. Immunol. 26(July 1996):1532-1538.

1701. A. Vanderplasschen, E. Mathew, M. Hollingshead, R.B. Sim, G.L. Smith, “Extracellular enveloped vaccinia virus is resistant to complement because of incorporation of host complement control proteins into its envelope,” Proc. Natl. Acad. Sci. (USA) 95(23 June 1998):7544-7549.

1702. G.L. Smith, “Vaccinia virus immune evasion,” Immunol. Lett. 65(January 1999):55-62.

1703. M. Marikovsky, M. Parizade, R. Arnon, Z. Fishelson, “Complement regulation on the surface of cultured schistosomula and adult worms of Schistosoma mansoni,” Eur. J. Immunol. 20(January 1990):221-227; M. Parizade, R. Arnon, P.J. Lachmann, Z. Fishelson, “Functional and antigenic similarities between a 94-kD protein of Schistosoma mansoni (SCIP-1) and human CD59,” J. Exp. Med. 179(1 May 1994):1625-1636.

1704. Z. Fishelson, “Novel mechanisms of immune evasion by Schistosoma mansoni,” Mem. Inst. Oswaldo Cruz 90(March-April 1995):289-292.

1705. Y. Ghendler, M. Parizade, R. Arnon, J.H. McKerrow, Z. Fishelson, “Schistosoma mansoni: evidence for a 28-kD membrane-anchored protease on schistosomula,” Exp. Parasitol. 83(June 1996):73-82.

1706. K. Iida, M.B. Whitlow, V. Nussenzweig, “Amastigotes of Trypanosoma cruzi escape destruction by the terminal complement components,” J. Exp. Med. 169(1 March 1989):881-891.

1707. L.L. Braga, H. Ninomiya, J.J. McCoy, S. Eacker, T. Wiedmer, C. Pham, S. Wood, P.J. Sims, W.A. Petri Jr., “Inhibition of complement membrane attack by the galactose-specific adhesin of Entamoeba histolytica,” J. Clin. Invest. 90(September 1992):1131-1137.

1708. L. Gutierrez-Kobeh, N. Cabrera, R. Perez-Montfort, “A mechanism of acquired resistance to complement-mediated lysis by Entamoeba histolytica,” J. Parasitol. 83(April 1997):234-241.

1709. W.L. Fodor, S.A. Rollins, E.R. Guilmette, E. Setter, S.P. Squinto, “A novel bifunctional chimeric complement inhibitor that regulates C3 convertase and formation of the membrane attack complex,” J. Immunol. 155(1 November 1995):4135-4138.

1710. J.N. Goldman, K.S. O’Rourke, J.D. McMannis, M.B. Goldman, “Effects of anti-C4 antibody on complement production by splenic and peritoneal macrophages,” Complement 5(1988):13-26.

1711. S.A. Rollins, L.A. Matis, J.P. Springhorn, E. Setter, D.W. Wolff, “Monoclonal antibodies directed against human C5 and C8 block complement-mediated damage of xenogeneic cells and organs,” Transplantation 60(15 December 1995):1284-1292.

1712. T.J. Kroshus, S.A. Rollins, A.P. Dalmasso, E.A. Elliott, L.A. Matis, S.P. Squinto, R.M. Bolman III, “Complement inhibition with an anti-C5 monoclonal antibody prevents acute cardiac tissue injury in an ex vivo model of pig-to-human xenotransplantation,” Transplantation 60(15 December 1995):1194-1202; Y. Wang, S.A. Rollins, J.A. Madri, L.A. Matis, “Anti-C5 monoclonal antibody therapy prevents collagen-induced arthritis and ameliorates established disease,” Proc. Natl. Acad. Sci. (USA) 92(12 September 1995):8955-8959; Y. Wang, Q. Hu, J.A. Madri, S.A. Rollins, A. Chodera, L.A. Matis, “Amelioration of lupus-like autoimmune disease in NZB/WF1 mice after treatment with a blocking monoclonal antibody specific for complement component C5,” Proc. Natl. Acad. Sci. (USA) 93(6 August 1996):8563-8568; T.C. Thomas, S.A Rollins, R.P. Rother, M.A. Giannoni, S.L. Hartman, E.A. Elliott, S.H. Nye, L.A. Matis, S.P. Squinto, M.J. Evans, “Inhibition of complement activity by humanized anti-C5 antibody and single-chain FV,” Mol. Immunol. 33(December 1996):1389-1401; H. Wang, S.A. Rollins, Z. Gao, B. Garcia, Z. Zhang, J. Xing, L. Li, R. Kellersmann, L.A. Matis, R. Zhong, “Complement inhibition with an anti-C5 monoclonal antibody prevents hyperacute rejection in a xenograft heart transplantation model,” Transplantation 68(15 December 1999):1643-1651.

1713. E.A. Amsterdam, G.L. Stahl, H.L. Pan, S.V. Rendig, M.P. Fletcher, J.C. Longhurst, “Limitation of reperfusion injury by a monoclonal antibody to C5a during myocardial infarction in pigs,” Am. J. Physiol. 268(1995):H448-H457.

1714. M.S. Mulligan, E. Schmid, B. Beck-Schimmer, G.O. Till, H.P. Friedl, R.B. Brauer, T.E. Hugli, M. Miyasaka, R.L. Warner, K.J. Johnson, P.A. Ward, “Requirement and role of C5a in acute lung inflammatory injury in rats,” J. Clin. Invest. 98(15 July 1996):503-512.

1715. E.L. Morgan, J.A. Ember, S.D. Sanderson, W. Scholz, R. Buchner, R.D. Ye, T. Hugli, “Anti-C5a receptor antibodies. Characterization of neutralizing antibodies specific for a peptide, C5aR-(9-29), derived from the predicted amino-terminal sequence of the human C5a receptor,” J. Immunol. 151(1 July 1993):377-388.

1716. G. Biesecker, C.M. Gomez, “Inhibition of acute passive transfer experimental autoimmune myasthenia gravis with Fab antibody to complement C6,” J. Immunol. 142(15 April 1989):2654-2659.

1717. Y. Kaneko, N. Okada, L. Baranyi, T. Azuma, H. Okada, “Antagonistic peptides against human anaphylatoxin C5a,” Immunology 86(September 1995):149-154.

1718. P.C. Astles, T.J. Brown, P. Cox, F. Halley, et al, “New nonpeptideic C5a receptor antagonists,” Bioorg. Medicinal Chem. Lett. 7(1997):907-912.

1719. X. Zhang, W. Boyar, N. Galakatos, N.C. Gonnella, “Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding,” Protein Sci. 6(January 1997):65-72.

1720. T.C. Pellas, W. Boyar, J. van Oostrum, J. Wasvary, et al, “Novel C5a receptor antogonists regulate neutrophil functions in vitro and in vivo,” J. Immunol. 160(1 June 1998):5616-5621; T.C. Pellas, L.P. Wennogle, “C5a receptor antagonists,” Curr. Pharm. Des. 5(October 1999):737-755.

1721. A.K. Wong, A.M. Finch, G.K. Pierens, D.J. Craik, S.M. Taylor, D.P. Fairlie, “Small molecular probes for G-protein-coupled C5a receptors: conformationally constrained antagonists derived from the C terminus of the human plasma protein C5a,” J. Medicinal Chem. 41(27 August 1998):3417-3425; A.M. Finch, A.K. Wong, N.J. Paczkowski, S.K. Wadi, D.J. Craik, D.P. Fairlie, S.M. Taylor, “Low-molecular-weight peptidic and cyclic antagonists of the receptor for the complement factor C5a,” J. Med. Chem. 42(3 June 1999):1965-1974.

1722. G. Biesecker, L. Dihel, K. Enney, R.A. Bendele, “Derivation of RNA aptamer inhibitors of human complement C5,” Immunopharmacology 42(May 1999):219-230.

1723. P. Phonimdaeng, M. O’Reilly, P. Nowlan, A.J. Bramley, T.J. Foster, “The coagulase of Staphylococcus aureus 8325-4. Sequence analysis and virulence of site-specific coagulase-deficient mutants,” Mol. Microbiol. 4(March 1990):393-404.

1724. M.K. Boden, J.I. Flock, “Fibrinogen-binding protein/clumping factor from Staphylococcus aureus,” Infect. Immun. 57(August 1989):2358-2363.

1725. M.K. Boden, J.I. Flock, “Evidence for three different fibrinogen-binding proteins with unique properties from Staphylococcus aureus strain Newman,” Microb. Pathog. 12(April 1992):289-298.

1726. M.K. Boden, J.I. Flock, “Cloning and characterization of a gene for a 19 kD fibrinogen-binding protein from Staphylococcus aureus,” Mol. Microbiol. 12(May 1994):599-606.

1727. D. McDevitt, P. Vaudaux, T.J. Foster, “Genetic evidence that bound coagulase of Staphylococcus aureus is not clumping factor,” Infect. Immun. 60(April 1992):1514-1523.

1728. B. Jansson, M. Uhlen, P.A. Nygren, “All individual domains of staphylococcal protein A show Fab binding,” FEMS Immunol. Med. Microbiol. 20(January 1998):69-78.

1729. J.P. Derrick, D.B. Wigley, “Crystal structure of a streptococcal protein G domain bound to an Fab fragment,” Nature 359(22 October 1992):752-754.

1730. S.Y. Cai, Y.Y. Wang, Z.J. Yao, “Structure analysis of streptococcal protein G Fc binding domain,” Sci. China B 36(January 1993):75-80.

1731. R.E. Baughn, “Role of fibronectin in the pathogenesis of syphilis,” Rev. Inect. Dis. 9(July-August 1987):S372-S385.

1732. P. Hagblom, E. Segal, E. Billyard, M. So, “Intragenic recombination leads to pilus antigenic variation in Neisseria gonorrhoeae,” Nature 315(9-15 May 1985):156-158.

1733. R.J. Belland, S.G. Morrison, J.H. Carlson, D.M. Hogan, “Promoter strength influences phase variation of neisserial opa genes,” Mol. Microbiol. 23(January 1997):123-135.

1734. G. Colman, “Streptococcus and Lactobacillus,” in M.T. Parker, B.I. Duerden, eds., Topley & Wilson’s Principles of Bacteriology, 8th Edition, Vol. 2, Systematic Bacteriology, E. Arnold, London, 1990, pp. 120-159.

1735. Ralph A. Giannella, “Salmonella,” in Samuel Baron, ed., Medical Microbiology, 4th Edition, University of Texas Medical Branch, 1996, Chapter 21; http://gsbs.utmb.edu/microbook/ch021.htm

1736. A.G. Barbour, “Antigenic variation of surface proteins of Borrelia species,” Rev. Infect. Dis. 10(July-August 1988):S399-S402.

1737. S.F. Lee, “Active release of bound antibody by Streptococcus mutans,” Infect Immun. 63(May 1995):1940-1946.

1738. K. Kobayashi, Y. Fujiyama, K. Hagiwara, H. Kondoh, “Resistance of normal serum IgA and secretory IgA to bacterial IgA proteases: evidence for the presence of enzyme-neutralizing antibodies in both serum and secretory IgA, and also in serum IgG,” Microbiol. Immunol. 31(1987):1097-1106.

1739. R. Ruchel, “Cleavage of immunoglobulins by pathogenic yeasts of the genus Candida,” Microbiol. Sci. 3(October 1986):316-319.

1740. J.C. Reeder, G.V. Brown, “Antigenic variation and immune evasion in Plasmodium falciparum malaria,” Immunol. Cell Biol. 74(December 1996):546-554.

1741. K.W. Deitsch, A. del Pinal, T.E. Wellems, “Intra-cluster recombination and var transcription switches in the antigenic variation of Plasmodium falciparum,” Mol. Biochem. Parasitol. 101(25 June 1999):107-116.

1742. D.R. Allred, “Antigenic variation in Babesia bovis: how similar is it to that in Plasmodium falciparum?” Ann. Trop. Med. Parasitol. 92(June 1998):461-472.

1743. C. Hetzel, R.M. Anderson, “The within-host cellular dynamics of bloodstage malaria: theoretical and experimental studies,” Parasitology 113(July 1996):25-38.

1744. C. Bogdan, M. Rollinghoff, “The immune response to Leishmania: mechanisms of parasite control and evasion,” Int. J. Parasitol. 28(January 1998):121-134.

1745. E. Handman, “Cell biology of Leishmania,” Adv. Parasitol. 44(1999):1-39.

1746. P.R. Murray, E.J. Baron, M.A. Pfaller, F.C. Tenover, R.H. Yoken, eds., Manual of Clinical Microbiology, 6th Edition, American Society for Microbiology, Washington DC, 1995.

1747. A. Nordstrand, A.G. Barbour, S. Bergstrom, “Borrelia pathogenesis research in the post-genomic and post-vaccine era,” Curr. Opin. Microbiol. 3(February 2000):86-92.

1748. M. Maass, J. Jahn, J. Gieffers, K. Dalhoff, H.A. Katus, W. Solbach, “Detection of Chlamydia pneumoniae within peripheral blood monocytes of patients with unstable angina or myocardial infarction,” J. Infect. Dis. 181(June 2000):S449-S451.

1749. J. Boman, C.A. Gaydos, “Polymerase chain reaction detection of Chlamydia pneumoniae in circulating white cells,” J. Infect. Dis. 181(June 2000):S452-S454.

1750. G. Rudenko, “Mechanisms mediating antigenic variation in Trypanosoma brucei,” Mem. Inst. Oswaldo Cruz 94(March-April 1999):235-237; R. McCulloch, J.D. Barry, “A role for RAD51 and homologous recombination in Trypanosoma brucei antigenic variation,” Genes Dev. 13(1 November 1999):2875-2888; P. Borst, W. Bitter, P.A. Blundell, I. Chaves, M. Cross, H. Gerrits, F. van Leeuwen, R. McCulloch, M. Taylor, G. Rudenko, “Control of VSG gene expression sites in Trypanosoma brucei,” Mol. Biochem. Parasitol. 91(1 March 1998):67-76; G. Rudenko, R. McCulloch, A. Dirks-Mulder, P. Borst, “Telomere exchange can be an important mechanism of variant surface glycoprotein gene switching in Trypanosoma brucei,” Mol. Biochem. Parasitol. 80(September 1996):65-75.

1751. Peter J. Eng, Thomas P. Trainor, Gordon E. Brown Jr., Glenn A. Waychunas, Matthew Newville, Stephen R. Sutton, Mark L. Rivers, “Structure of the Hydrated alpha-Al2O3 (0001) Surface,” Science 288(12 May 2000):1029-1033.

1752. David Malakoff, “Aluminum Is Put on Trial as A Vaccine Booster,” Science 288(26 May 2000):1323-1324.

1753. Elizabeth J. Harfenist, Robert K. Murray, “Chapter 59. Plasma Proteins, Immunoglobulins, & Blood Coagulation,” in Robert K. Murray, Daryl K. Granner, Peter A. Mayes, Victor W. Rodwell, eds., Harper’s Biochemistry, 23rd Edition, Appleton & Lange, Norwalk CT, 1993, pp. 665-687.

1754. Gary Taubes, “Ways to Vary the Gene Vaccine Theme,” Science 278(5 December 1997)1713.

1755. Gustav J.V. Nossal, “Life, Death and the Immune System,” Scientific American (September 1993):53-62.

1756. Daniel C. Adelman, Abba Terr, “Allergic and Immunologic Disorders,” in Lawrence M. Tierney, Jr., Stephen J. McPhee, Maxine A. Papadakis, eds., Current Medical Diagnosis and Treatment, 35th Edition, Appleton and Lange, Stamford, CT, 1996, pp. 694-718.

1757. Thomas J. Spira, “Immunodeficiency involving B-cell function,” in J. Willis Hurst. ed., Medicine for the Practicing Physician, Third Edition, Butterworth-Heinemann, Boston MA, 1992, pp. 146-148.

1758. Nick Holmes, “Antigen Recognition: B Cells and Antibodies,” 10 September 1999, University of Cambridge, Department of Pathology, Immunology Division; http://www-immuno.path.cam.ac.uk/~immuno/part1/lec06/lec6_97.html

1759. Ivan Roitt, Jonathan Brostoff, David Male, Immunology, Fourth Edition, Mosby, London, 1996.

1760. Eli Benjamini, Richard Coico, Geoffrey Sunshine, Immunology: A Short Course, Fourth Edition, John Wiley & Sons, Inc., New York, 2000.

1761. J. Roes, K. Rajewsky, “Immunoglobulin D (IgD)-deficient mice reveal an auxiliary receptor function for IgD in antigen-mediated recruitment of B cells,” J. Exp. Med. 177(1 January 1993):45-55.

1762. C. Lutz, B. Ledermann, M.H. Kosco-Vilbois, A.F. Ochsenbein, R.M. Zinkernagel, G. Kohler, F. Brombacher, “IgD can largely substitute for loss of IgM function in B cells,” Nature 393(25 June 1998):797-801.

1763. Anthony P. Weetman, Leslie J. DeGroot, “Chapter 7. Autoimmunity to the Thyroid Gland,” in The Thyroid and its Diseases, 1 January 2000; http://www.thyroidmanager.org/Chapter7/7-text.htm

1764. T. Petteri Arstila, Armanda Casrouge, Veronique Baron, Jos Even, Jean Kanellopoulos, Philippe Kourilsky, “A Direct Estimate of the Human alphabeta T Cell Receptor Diversity,” Science 286(29 October 1999):958-961.

1765. Lubert Stryer, Biochemistry, 4th Edition, W.H. Freeman and Company, New York, 1995.

1766. Philipp Holliger, Hennie R. Hoogenboom, “Artificial Antibodies and Enzymes: Mimicking Nature and Beyond,” Trends in Biotechnology 13(January 1995):7-9.

1767. Ariel G. Loewy, Philip Siekevitz, John R. Menninger, Jonathan A.N. Gallant, Cell Structure and Function: An Integrated Approach, Third Edition, Saunders College Publishing, Philadelphia PA, 1991.

1768. K. Landsteiner, The Specificity of Serological Reactions, Harvard University Press, Cambridge, MA, 1946.

1769. T.A. Desai, W.H. Chu, J.K. Tu, G.M. Beattie, A. Hayek, M. Ferrari, “Microfabricated immunoisolating biocapsules,” Biotechnol. Bioeng. 57(5 January 1998):118-120; Tejal A. Desai et al, “Nanopore Technology for Biomedical Applications,” J. Biomed. Microdevices 2(1999):11-40; see also: http://www.uic.edu/depts/bioe/faculty/tejal_desai/publications.htm

1770. K.P. Peterson, C.M. Peterson, E.J. Pope, “Silica sol-gel encapsulation of pancreatic islets,” Proc. Soc. Exp. Biol. Med. 218(September 1998):365-369.

1771. E. Rafael, A. Wernerson, P. Arner, G.S. Wu, A. Tibell, “In vivo evaluation of glucose permeability of an immunoisolation device intended for islet transplantation: a novel application of the microdialysis technique,” Cell Transplant. 8(May-June 1999):317-326; Ehab Rafael, “Cell transplantation and immunoisolation: Studies on a macroencapsulation device,” dissertation 99:698, Karolinska Institutet, 17 December 1999; http://diss.kib.ki.se/1999/91-628-3883-0/

1772. T.T. Ton-That, D. Doron, B.S. Pollard, J. Bacher, H.B. Pollard, “In vivo bypass of hemophilia A coagulation defect by Factor XIIa implant,” Nat. Biotechnol. 18(March 2000):289-295.

1773. J.M. Verdier, K.V. Ewart, M. Griffith, C.L. Hew, “An immune response to ice crystals in North Atlantic fishes,” Eur. J. Biochem. 241(1 November 1996):740-743.

1774. N. Kessler, D. Perl-Treves, L. Addadi, “Monoclonal antibodies that specifically recognize crystals of dinitrobenzene,” FASEB J. 10(October 1996):1435-1442.

1775. D.R. Davies, G.H. Cohen, “Interactions of protein antigens with antibodies,” Proc. Natl. Acad. Sci. (USA) 93(9 January 1996):7-12.

1776. W.R. Tulip, J.N. Varghese, W.G. Laver, R.G. Webster, P.M. Colman, “Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex,” J. Mol. Biol. 227(5 September 1992):122-148; J.N. Varghese, W.G. Laver, P.M. Colman, “Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution,” Nature 303(5-11 May 1983):35-40.

1777. M. Kam, D. Perl-Treves, R. Sfez, L. Addadi, “Specificity in the recognition of crystals by antibodies” J. Mol. Recognit. 7(December 1994):257-264; M. Kam, D. Perl-Treves, D. Caspi, L. Addadi, “Antibodies against crystals,” FASEB J. 6(May 1992):2608-2613.

1778. N. Kessler, D. Perl-Treves, L. Addadi, M. Eisenstein, “Structural and chemical complementarity between antibodies and the crystal surfaces they recognize,” Proteins 34(15 February 1999):383-394.

1779. D. Perl-Treves, N. Kessler, D. Izhaky, L. Addadi, “Monoclonal antibody recognition of cholesterol monohydrate crystal faces,” Chem. Biol. 3(July 1996):567-577.

1780. J.J. Mond, A. Lees, C.M. Snapper, “T cell-independent antigens type 2,” Annu. Rev. Immunol. 13(1995):655-692.

1781. J. Fauque, J.L. Borgna, H. Rochefort, “A monoclonal antibody to the estrogen receptor inhibits in vitro criteria of receptor activation by an estrogen and an anti-estrogen,” J. Biol. Chem. 260(15 December 1985):15547-15553.

1782. A. Vincenot, J.L. Pittet, M. Aiach, P. Gaussem, “A monoclonal antibody recognizing the activation domain of protein C in its calcium-free conformation,” FEBS Lett. 432(31 July 1998):94-97.

1783. M.L. Fu, P.S. Leung, G. Wallukat, G. Bergstrom, H. Fu, W. Schulze, H. Herlitz, “Agonist-like activity of antibodies to angiotensin II receptor subtype 1 (AT1) from rats immunized with AT1 receptor peptide,” Blood Press. 8(1999):317-324.

1784. T. Kimura, T. Hosoi, K. Yamamoto, N. Suzuki, Y. Imai, T. Irimura, “Epitope mapping of monoclonal antibodies specific for a macrophage lectin: a calcium-dependent epitope is in the carbohydrate recognition domain,” Mol. Immunol. 37(1 February 2000):151-160.

1785. L.M. Wright, A.M. Brzozowski, R.E. Hubbard, A.C. Pike, S.M. Roberts, R.N. Skovgaard, I. Svendsen, H. Vissing, R.P. Bywater, “Structure of fab hGR-2 F6, a competitive antagonist of the glucagon receptor,” Acta Crystallogr. D Biol. Crystallogr. 56(May 2000):573-580.

1786. J.D. Radolf, M.V. Norgard, W.W. Schulz, “Outer membrane ultrastructure explains the limited antigenicity of virulent Treponema pallidum,” Proc. Natl. Acad. Sci. (USA) 86(March 1989):2051-2055.

1787. J.F. Bohnsack, X.N. Zhou, J.N. Gustin, C.E. Rubens, C.J. Parker, H.R. Hill, “Bacterial evasion of the antibody response: human IgG antibodies neutralize soluble but not bacteria-associated group B streptococcal C5a-ase,” J. Infect. Dis. 165(February 1992):315-321.

1788. N. Burman, A. Shamaei-Tousi, S. Bergstrom, “The spirochete Borrelia crocidurae causes erythrocyte rosetting during relapsing fever,” Inect. Immun. 66(February 1998):815-819.

1789. R. Ramasamy, S. Yasawardena, R. Kanagaratnam, E. Buratti, F.E. Baralle, M.S. Ramasamy, “Antibodies to a merozoite surface protein promote multiple invasion of red blood cells by malaria parasites,” Parasite Immunol. 21(August 1999):397-407.

1790. L.F. Qualtiere, A.G. Anderson, P. Meyers, “Effects of ionic and nonionic detergents on antigen-antibody reactions,” J. Immunol. 119(November 1977):1645-1651; H.H. Weetall, J. Bozicevich, “Effect of surfactants on antigen-antibody reactions,” Nature 215(30 September 1967):1479-1480.

1791. P.E. Darwin, M.B. Sztein, Q.X. Zheng, S.P. James, G.T. Fantry, “Immune evasion by Helicobacter pylori: gastric spiral bacteria lack surface immunoglobulin deposition and reactivity with homologous antibodies,” Helicobacter 1(March 1996):20-27.

1792. P. Pouedras, P.M. Andre, P.Y. Donnio, J.L. Avril, “Cleavage of immunoglobulin A1, A2 and G by proteases from clinical isolates of Pasteurella multocida,” J. Med. Microbiol. 37(August 1992):128-132.

1793. A. Kharazmi, “Mechanisms involved in the evasion of the host defence by Pseudomonas aeruginosa,” Immunol. Lett. 30(October 1991):201-205.

1794. A. Molla, T. Kagimoto, H. Maeda, “Cleavage of immunoglobulin G (IgI) and IgA around the hinge region by proteases from Serratia marcescens,” Infect. Immun. 56(April 1988):916-920.

1795. S. Cohen, “Survival of pathogenic organisms in immunocompetent hosts,” Chemioterapia 4(August 1985):329-338.

1796. Y. Yamaguchi, H. Kim, K. Kato, K. Masuda, I. Shimada, Y. Arata, “Proteolytic fragmentation with high specificity of mouse immunoglobulin G. Mapping of proteolytic cleavage sites in the hinge region,” J. Immunol. Methods 181(26 April 1995):259-267.

1797. J. Reinholdt, “A method for titration of inhibiting antibodies to bacterial immunoglobulin A1 proteases in human serum and secretions,” J. Immunol. Methods 191(10 May 1996):39-48.

1798. T. Fehr, M.F. Bachmann, E. Bucher, U. Kalinke, F.E. Di Padova, A.B. Lang, H. Hengartner, R.M. Zinkernagel, “Role of repetitive antigen patterns for induction of antibodies against antibodies,” J. Exp. Med. 185(19 May 1997):1785-1792, 1721-1723 (comment).

1799. N.K. Jerne, “Idiotypic networks and other preconceived ideas,” Immunol. Rev. 79(June 1984):5-24.

Last updated on 16 April 2004