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Figure 1.
(a) RSV neutralization curves for palivizumab and motavizumab
IgG as determined by a flow cytometric assay. (b) Surface
representation of the Fab and ribbon representation of the
peptide, viewed looking down at the CDRs and a 90° rotation
about the horizontal axis from c and d. (c) Interactions between
the peptide and six Fab CDRs. Side chains are shown for those
residues making intermolecular interactions. Dashed lines
represent hydrogen bonds. Residues in the hydrophobic patch on
the heavy chain are shown with transparent surfaces. These
include Trp52 and Trp53 on the right and Ile97, Phe98 and Phe100
on the left. (d) Motavizumab mutations that alter affinity to
the F glycoprotein. Side chains are shown for those Fab residues
that increase affinity by directly contacting the peptide (red),
by altering the position of residues that directly contact the
peptide (cyan) or by binding to the F glycoprotein outside the
primary epitope or enhancing long-range electrostatic
interactions (magenta). Fab residues in yellow decrease the
affinity for the F glycoprotein but increase in vivo potency
compared to an earlier version of motavizumab.
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