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The CD147–Cyclophilin A (CypA) protein–protein interface is a critical signaling node involved in inflammatory responses and tissue remodeling. CD147, also known as Basigin or EMMPRIN, is a transmembrane glycoprotein that acts as the primary cell-surface receptor for extracellular CypA, a peptidyl-prolyl isomerase (UniProt P35613, P62937). This interaction triggers intracellular signaling cascades, such as the MAPK/ERK pathway, leading to the upregulation of matrix metalloproteinases (MMPs) and the promotion of leukocyte chemotaxis (PubMed: 22917007). Pathologically, this interface plays a significant role in various conditions, including rheumatoid arthritis, cardiovascular diseases like atherosclerosis, and the progression of several cancers (PubMed: 24552670). Furthermore, the CD147–CypA interaction has been implicated in the entry mechanisms of several viruses, including SARS-CoV-2 and HIV-1 (PubMed: 33273462). Therapeutic strategies targeting this interface include monoclonal antibodies against CD147, such as Meplazumab, and small-molecule inhibitors designed to block the binding site, aiming to mitigate chronic inflammation and viral pathogenesis.
Inhibition of the protein-protein interaction between extracellular Cyclophilin A and the CD147 receptor to block downstream inflammatory signaling and matrix metalloproteinase production.
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