Download Idiotypes in Medicine: Autoimmunity, Infection and Cancer. by R. C. Kennedy, S. Ferrone, Yehuda Shoenfeld PDF

By R. C. Kennedy, S. Ferrone, Yehuda Shoenfeld

This is often the main entire overview of the idiotypic community on hand. all of the present wisdom of idiotypes of some of the antibodies is included during this quantity. The pathogenic position of idiotypes in autoimmunity and melanoma is reviewed extensive. The healing half focusses on harnessing anti-idiotypes for treating autoimmunological issues, and at the employment of idiotypes for vaccines in melanoma and infectious ailments, in addition to explaining the manipulation of the idiotypic community in autoimmunity and melanoma idiotypes and vaccines.

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Extra resources for Idiotypes in Medicine: Autoimmunity, Infection and Cancer. Autoimmunity, Infection and Cancer

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On the nature of allosteric transitions: a plausible model. J Mol Biol 1965; 12: 88-119. Morgan RS, Miller SL, McAdon JM. The symmetry of self complementary surfaces. J Mol Biol 1979;127:31-39. Padlan EA. Anatomy of the antibody molecule. Mol Immunol 1994;31:169-217. Pain D, Murakami H, Blobel G. Identification of a receptor for protein import into mitochondria. Nature (London), 1990;347:444-449. Pan Y, Yuhasz SC, Amzel M. Anti-idiotypic antibodies: biological function and structural studies. FASEB J 1995;9:43-49.

Interestingly, solvent molecules contribute to the binding mimicry. 3—lysozyme interfaces. Interactions between the two different Id—anti-Id complexes and an antigen—antibody complex are compared in Figure 2 (p. A and B (p. 30). THE ANTI-FELINE INFECTIOUS PERITONITIS VIRUS SYSTEM For this idiotope-anti-idiotope system the original antigen was the E2 peplomer, a large glycoprotein, of feline infectious peritonitis virus (FIPV). The E2 peplomer was chosen as an antigen because it is responsible for: a) the binding of virus to plasma membranes of susceptible cells, b) cell fusion, c) induction of cell-mediated cytotoxicity of infected cells, and d) induction of neutralizing antibody (Sturman and Holmes, 1983).

Sizes of hypervariable regions are according to the structural classification of Chothia (38), except for loops H3 which follow the convention of Kabat (39). 5 A. 29 Table 1. A. 1 (Abl) T91AJ5(Ab2)- LI Y30 Y32 Y50 G91 N92 Wj^90(lH) Y„59(1H) Y^IOO(IH) 8^30(1 H) L2 FR3 L3 H2 H3 B. 3 (Ab2)-- LI L2 L3 D28 R66 H91 Y92 S93 T94 F96 T30 Sj^28(4, IH) S^28(l) 30 FH102(2) N^59(l, IH) G,92(l) F„102(4) RL30(7) Y„32(1H) HI Y^94(10) Wj^33(5) q 9 1 ( 2 , IH) L„100(3) Y„52(8) SH55(1) D„57(5, IH) D^57(3, IH) Gj^92(2, IH) N53 K54 D56 E61 MJ» Lysozyme (Ag) QHUIH) RL45(1H) SL91(1H) YL48(1H) K,52(1H) YH98(2) S^28(3) S,31(3) Y„99(l) YH98(4) F,97(3) 1,29(8) D.

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