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. 2023 Apr 21;15(6):e17454. doi: 10.15252/emmm.202317454

Figure 2. C‐CSP specific mAbs are frequently encoded by IGHV3‐21 .

Figure 2

  1. SPR affinity of C‐CSP reactive mAbs.
  2. Frequency of mAbs encoded by the indicated IGHV and IGKV or IGLV pairs.
  3. VH SHM load of VH3‐21 and non‐VH3‐21 mAbs. mAbs with unmutated VH are highlighted in green; n indicates the number of mAbs tested.
  4. Amino acid (aa) VH replacement (red bars) and silent (black bars) SHM in VH3‐21 mAbs (n = 113). FWR, framework region; CDR, complementarity‐determining region.
  5. Observed (Obs) aa usage frequency at position H.31 and H.33 in VH3‐21 mAbs carrying a replacement mutation at these positions compared to the expected (Exp) neutral mutation model (Yaari et al, 2013; Gupta et al, 2015). Single‐letters indicate aa residues: G, Gly; I, Ile; N, Asn; R, Arg; T, Thr.
  6. C‐CSP affinity for selected VH3‐21 mAbs with or without Thr mutation at position H.33.

Data information: The statistical significance in (F) was assessed by two‐tailed Mann–Whitney test: **P = 0.0019. Red horizontal lines in (A, F) indicate geometric mean values. Data in (A, C and F) are representative of two independent technical replicates.

Source data are available online for this figure.