Signaling lymphocytic activation molecule (SLAMF1), Nectin cell adhesion molecule 4 (Nectin-4), and Membrane cofactor protein (CD46) (SLAMF1/Nectin-4/CD46)

The host cell receptors for measles virus entry comprise a group of surface proteins that facilitate the attachment and internalization of the virus into various tissues. The primary receptors include signaling lymphocytic activation molecule (SLAMF1), which is expressed on immune cells and serves as the entry point for wild-type strains, and nectin cell adhesion molecule 4 (Nectin-4), which is located on epithelial cells and is essential for viral shedding and transmission (1.2.1, 1.4.1). Additionally, membrane cofactor protein (CD46) is utilized by vaccine and laboratory-adapted strains for entry into a wide range of nucleated cells (1.2.3, 1.4.2). These receptors interact with the viral hemagglutinin protein, triggering a conformational change in the fusion protein that leads to membrane merger (1.3.2, 1.3.4). Therapeutic strategies targeting these receptors include the use of antibody-drug conjugates like enfortumab vedotin for Nectin-4-positive cancers and experimental entry inhibitors designed to prevent viral infection (1.1.1, 1.2.4). Understanding these interactions is crucial for both antiviral development and the engineering of oncolytic viruses that exploit receptor overexpression in tumors.

Other names

CD150SLAMPVRL4MCPSignaling lymphocyte activation moleculePoliovirus receptor-related 4Membrane cofactor proteinCD46

Antibody-drug conjugate targeting Nectin-4 and inhibition of viral entry through receptor blockade.