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Contact: t-wu@nwu.edu Rheumatoid factors are auto-antibodies which bind the Fc portion of autologous immunoglobulin G molecules. Since the etiology of the production of such autoantibodies is unclear, we try to match the amino acid and nucleotide sequences of their heavy chain third complementarity determining (CDRH3) and fourth framework (FRH4) regions to other antibodies with known specificities, in the hope of discovering possible underlying mechanisms for their aberrant production. Variable regions of antibody heavy chains are coded by gene segments formed by D–J re-arrangement with possible intervening Nand/or P-segments, followed by the joining of a V-gene to the 5′-end of the D-minigene also with possible intervening Nand/or P-segments (Slackman et al., 1996). The 3′-end of V-gene, Dand J-minigenes, together with the Nand/or P-segments, code for the CDRH3-FRH4 segment. CDRH3 confers fine specificity to the antibody (Kabat et al., 1991) in the sense that a given amino acid sequence of entire CDRH3 consisting of five or more residues is always associated with a unique antibody specificity. The other five CDRs, in general, provide higher binding affinity by providing geometrical restrictions (VargasMadrazo et al., 1995) and surface interactions. CDRH3 sequences of mouse rheumatoid factors may thus provide some clue as to how such auto-antibodies can be generated. Experimentally, IgG-Fc binding rheumatoid factors can be produced in the mouse with certain protein (Shlomchik et al., 1987) or carbohydrate (Stanley et al., 1992) antigens. However, the challenging antigens are usually quite different structurally from the Fc portions of autologous IgG molecules. Thus, molecular mimicry (Oldstone,

Matching amino acid and nucleotide sequences of mouse rheumatoid factor CDRH3-FRH4 segments to other mouse antibodies with known specificities