CD147–Cyclophilin A complex

The CD147–Cyclophilin A complex is formed by the interaction between Cyclophilin A (CypA), a peptidyl-prolyl cis-trans isomerase with chaperone activity, and CD147 (also known as Basigin, BSG, or EMMPRIN), a type I transmembrane glycoprotein of the immunoglobulin superfamily. Extracellular Cyclophilin A binds to CD147 on the surface of multiple cell types, activating pro-inflammatory and pro-tumorigenic signaling pathways. This complex facilitates cell signaling, regulates cell proliferation, and plays essential roles in the progression of cancer, inflammatory disorders, and viral infections such as HIV-1 and SARS-CoV by promoting viral entry and replication. Both CD147 and Cyclophilin A are validated therapeutic targets, and disruption of this interaction is under investigation for cancer and viral disease treatment. Overexpression of either component is associated with poor prognosis in several cancers. Drug development efforts focus on blocking this protein–protein interaction or the enzymatic function of Cyclophilin A to modulate disease progression.

Other names

CD147–CypA complexBasigin–Cyclophilin A complexEMMPRIN–Cyclophilin A complexBSG–Cyclophilin A complex

Inhibition of cyclophilin A peptidyl-prolyl isomerase activity. Disruption of Cyclophilin A–CD147 interaction blocks downstream signaling. Modulation of immune cell chemotaxis and inflammation. Inhibition of viral entry (e.g., preventing HIV-1 and SARS-CoV infection).