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Color Plates

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Figure 1

(See p. 75.) Inflammatory heart disease in BALB/c mice that were immunized with the endogenous mouse M7Aα peptide from the α myosin heavy chain (A), the control endogenous M7Aβ peptide from the homologous region of the β-myosin heavy chain (B), the 60-kDa CRP-derived peptide from (ChTRl) (C), and the 60-kDa CRP-derived peptide from (ChPN) (D) (1). Hearts were analyzed 21 days after the initial immunization. Hematoxylin-eosin staining was used. Magnifications, ×320.

Citation: Cunningham M, Fujinami R. 2000. Color Plates, In Molecular Mimicry, Microbes, and Autoimmunity. ASM Press, Washington, DC.
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Figure 2

(See p. 79.) Blood vessels in mice immunized with 60-kDa CRP-derived peptide. (A) Thickening of the arterial wall and perivascular fibrotic changes in mice immunized with ChTR1. Note the perivascular mononuclear inflammatory cells. (B) Normal morphology of the cardiac artery in mice immunized with Freud's complete adjuvant (FCA) alone. (C) Occlusion of cardiac blood vessels in mice immunized with ChTRl. (D) No occlusions in cardiac blood vessel were seen in control mice immunized with FCA alone. (A and B) Elastica staining for collagen (red) for detection of fibrotic changes. (C and D) Hematoxylin-eosin staining was used. Magnifications, ×320.

Citation: Cunningham M, Fujinami R. 2000. Color Plates, In Molecular Mimicry, Microbes, and Autoimmunity. ASM Press, Washington, DC.
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Figure 6

(See p. 154.) Crystal structure of PAl bound to MAb 2H1. (A) Looking down on PAl resting in the binding site of 2H1, which is shown in white, with positively charged regions in blue and negatively charged areas in red. Antibody heavy-chain CDR2 and CDR3 and light-chain CDR1 and CDR3 are denoted by H2. H3, LI, and L3, respectively. (B) Side view showing the cutaway surface of MAb 2H1 in white and the molecular surface of PAl as a lilac mesh. The orientation of the peptide is similar to that in panel A, and the residues corresponding to the PAl motif are colored as follows: T5, blue-green; P6, purple; W8, pink; M9. orange: L10. green. The remainder of the peptide is shown in yellow. The surfaces of two cavities between the antibody and the bound peptide are colored yellow, green, and orange according to their proximity to the antibody light chain, antibody heavy chain, and peptide, respectively.

Citation: Cunningham M, Fujinami R. 2000. Color Plates, In Molecular Mimicry, Microbes, and Autoimmunity. ASM Press, Washington, DC.
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Figure 1

(See p. 203.) Crystal structure of the complex of HLA-DR2 and the MBP peptide (residues 85 to 99). (A) Overview of the structure. MBP peptide residues V89, F92,195. and T97 occupy the P1, P4, P6, and P9 pockets of the HLA-DR2 binding site, respectively. (B) Solvent-exposed residues that are important for TCR recognition of the MBP peptide (residues 85 to 99). MBP residues H90, F91. and K93 were identified as important TCR contact residues. These are located at the P2, P3, and P5 positions, respectively, and are available for interaction with the TCR. (C) P4 pocket of the HLA-DR2 binding site. This pocket is occupied by F92 of the MBP peptide. The necessary room for this aromatic side chain is created by the DRβ71 polymorphism. (D) Close-up view of MBP peptide residues that are important for TCR recognition. Preferences at positions P-l, P2, P3, and P5 were considered in the search criteria for cross-reactive microbial peptides. Reprinted from (57) with permission of the publisher.

Citation: Cunningham M, Fujinami R. 2000. Color Plates, In Molecular Mimicry, Microbes, and Autoimmunity. ASM Press, Washington, DC.
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Figure 2

(See p. 205.) Electron density and model of the MBP peptide in the binding site of HLA-DR2. (A) Electron density of the MBP peptide bound to HLA-DR2. The C terminus of the peptide (P10, PI 1) is partially disordered. (B) Superposition of the two MBP peptides in the asymmetric unit. The DR2-MBP peptide complex crystallized as a dimer of dimers, like other HLA-DR molecules (4, 61). The model for the MBP peptide includes residues P-3 to PI 1 and P-4 to P10 for the two copies in the asymmetric unit, yellow and blue, respectively. The peptide backbones superimpose in the P-l to P4 segment and are more divergent in the C-terminal segment due to different crystal contacts. A crystal contact between peptide residue P-3 in one molecule and P5 from a symmetrically related molecule stabilizes the N terminus of one peptide, enabling P-4 to be included in the model for this peptide and P5 Lys to be included in the model for the other peptide. Reprinted from (57) with permission of the publisher.

Citation: Cunningham M, Fujinami R. 2000. Color Plates, In Molecular Mimicry, Microbes, and Autoimmunity. ASM Press, Washington, DC.
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