Affinity Analysis of CD16a- IgG Ligands Interactions - Abstract
CD16a is the most key antibody Fc receptor expressed on human natural killer (NK) cells
and is responsible to trigger NK cell-mediated ADCC. Therapeutic monoclonal antibodies
(mAbs) require binding to CD16a for full effect and increasing the binding affinity. The point
mutants were introduced into SCD1, CD16A mimetics, to enhance the binding affinity with
IgG Fc fragment. Their three-dimensional structures were determined by homology modeling
based on results previously determined by X-ray crystallography. The binding models were
carried out via protein-protein docking tools. The best docking solutions were retained based
on the docking scores and were used for structural assessment. Our results indicated that
mutations in the CD16A receptor could strengthen binding affinity with IgG Fc fragment and
might improve the interaction pattern of the neighboring residues. The stabilized mimetics of the
small-molecule CD16A should serve as a promising target for bispecific antibodies that target
the HIV-1 envelope protein and viral entry inhibitor.