Autoreactivity and Exceptional CDR Plasticity (but Not Unusual Polyspecificity) Hinder Elicitation of the Anti-HIV Antibody 4E10
Figure 8
Top scoring 4E10 and b12 PhIP-Seq 36-mer peptides.
The top fifteen scoring 36-mer peptides from the b12 IgG PhIP-Seq analysis (above) and the seventeen top scoring 36-mer peptides from the 4E10 IgG analysis exceeding the threshold set by the highest-scoring b12 peptide (below) are shown, compiled by their relative rank order, replicate-averaged PhIP-Seq score, sequence, identity of the parent protein, hydrophobicity (Φ) and predicted charge at neutral pH. Hydrophobicities were determined with the Sigma-Aldrich PEPscreen Library Design Tool (green: hydrophilic; orange: moderately hydrophobic; red: hydrophobic; no peptides were predicted to be “very hydrophobic”); overall charge was determined with the Innovagen Peptide Property Calculator (red: negative; green: neutral; blue: positive). Segments of low sequence complexity (defined by the program SEG [112]) are highlighted in red; the core motif in the IP3R isoform peptides (labeled in bold), identified by MEME [72], is underlined. Asterisks indicate peptide sequences selected for expression as fusion constructs for subsequent validation.