Figure 1

The structures of TCRβ CDR3 region of E7, C5 or non-peptide/HLA-DR tetramers-bound CD4⁺ T cells in PLF13 and comparison of amino-acid sequences’ length of TCRβ CDR3 of E7/HLA-DR-bound CD4⁺ T cells. (a) The protein tertiary structures of E7/HLA-DR tetramers 2#, 11#, and 12# bound CD4⁺ TCRβ CDR3 region, area between the arrows. Although amino-acid sequences are different, the CDR3 protein tertiary structure showed similar each other in PLF13 as long as the peptide E7 binds; (b) The protein tertiary structures of C5/HLA-DR tetramers 6#, 15#, and 16# bound CD4⁺ TCRβ CDR3 region. The structure of C5-bound CD4⁺ TCRβ CDR3 region showed another shape of structure, which was distinct from those of E7-bound CD4⁺ T cells; (c) The protein tertiary structures of E7/HLA-DR tetramers AK2#, AK11#, and AK12# bound CD4⁺ TCRβ CDR3 region. Non-peptide tetramers bound CD4⁺ T cells TCRβ CDR3 tertiary structures were entirely different each other. In a, b, and c, all structures were oriented with CDR3 region in the top left corner. According to the number of tetramers, structures, from left to right, corresponded to their respective amino-acid sequences; (d) Eleven TB patients were included in this study (clones = 252). Frequency histograms of TCRβ CDR3 amino-acid sequences were shown. For patients, the count of TCRβ CDR3 amino-acid sequences’ length of E7-bound CD4⁺ T cells in total sequence results was calculated (Y axis), which focused on 5 to 19 amino-acid residues (X axis), mainly distributed in 12 amino-acid sequences.