Abstract
NK cells are an important arm of the innate immune system, and they
constitutively express the NKp30 receptor. NKp30-mediated responses are
triggered by the binding of specific ligands, such as tumour
cell-derived B7-H6, and involve the secretion of cytotoxic mediators
TNF-α, IFN-γ, perforins and granzymes. The latter two constitute a
target cell-directed response that is critical in the process of
immunosurveillance. The structure of NKp30 is presented, focusing on the
ligand-binding site, on the ligand-induced structural changes, and on
the experimental data available correlating structure and binding
affinity. The translation of NKp30 structural changes to disease
progression is also reviewed. NKp30 role in immunotherapy has been
explored in chimeric antigen receptor T-cell (CAR-T) therapy. However,
antibodies or small ligands targeting NKp30 have not yet been developed.
The data reviewed unveils the key structural aspects that must be
considered for drug design in order to develop novel immunotherapy
approaches.