Erythrocyte invasion-neutralising antibodies prevent RH5 from binding to basigin-containing membrane protein complexes.

Basigin is an essential host receptor for invasion of into human erythrocytes, interacting with parasite surface protein PfRH5. PfRH5 is a leading blood-stage malaria vaccine candidate and a target of growth-inhibitory antibodies. Here, we show that erythrocyte basigin is exclusively found in one of two macromolecular complexes, bound either to plasma membrane Ca-ATPase 1/4 (PMCA1/4) or to monocarboxylate transporter 1 (MCT1).

Neuroplastin and Basigin Are Essential Auxiliary Subunits of Plasma Membrane Ca-ATPases and Key Regulators of Ca Clearance.

Plasma membrane Ca-ATPases (PMCAs), a family of P-type ATPases, extrude Ca ions from the cytosol to the extracellular space and are considered to be key regulators of Ca signaling. Here we show by functional proteomics that native PMCAs are heteromeric complexes that are assembled from two pore-forming PMCA1-4 subunits and two of the single-span membrane proteins, either neuroplastin or basigin. Contribution of the two Ig domain-containing proteins varies among different types of cells and along postnatal development.