Measles virus entry receptors (MeV receptors)

Measles virus entry receptors are host cell surface proteins that the measles virus (MeV) exploits to bind and enter target cells. The two primary receptors for wild-type MeV are Signaling Lymphocytic Activation Molecule Family Member 1 (SLAMF1, also known as CD150) and Nectin-4 (also known as PVRL4). SLAMF1 is expressed on various immune cells, such as activated T and B cells, dendritic cells, and macrophages, and is responsible for the initial infection and systemic spread of the virus (Tatsuo et al., 2000). Nectin-4 is an adherens junction protein found on the basolateral surface of epithelial cells in the respiratory tract, facilitating viral exit and transmission to new hosts (Mühlebach et al., 2011). Additionally, vaccine and laboratory-adapted strains of MeV can utilize Membrane Cofactor Protein (CD46), a ubiquitously expressed complement regulator, as an entry receptor (Naniche et al., 1993). These receptors are significant therapeutic targets; for example, Nectin-4 is targeted by the antibody-drug conjugate enfortumab vedotin in cancer therapy, while fusion-blocking peptides and small molecules are being researched to inhibit MeV entry by disrupting the interaction between the viral hemagglutinin protein and these host receptors.

Other names

Signaling lymphocytic activation molecule family member 1SLAMF1CD150SLAMNectin-4PVRL4Poliovirus receptor-like 4LNIRMembrane cofactor proteinCD46MCP

Entry inhibition by blocking viral attachment to host receptors, fusion inhibition, and targeted cytotoxicity via antibody-drug conjugates.