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The host cell receptors for measles virus entry are a group of cell surface proteins that facilitate the infection of various human tissues by the measles virus (MeV) (Lin et al., 2016). The primary receptor for wild-type MeV on immune cells is Signaling Lymphocytic Activation Molecule Family Member 1 (SLAMF1, also known as CD150), which is expressed on activated T and B cells, dendritic cells, and macrophages (Lin et al., 2016; Muhlebach et al., 2012). For infection of epithelial cells, the virus utilizes Nectin-4 (PVRL4), an adherens junction protein that also serves as a significant biomarker and therapeutic target in several adenocarcinomas (Muhlebach et al., 2011). Additionally, vaccine and laboratory-adapted strains of MeV can utilize Membrane Cofactor Protein (CD46), a complement regulatory protein found on all nucleated cells (Gerlier et al., 1995). These receptors interact with the viral hemagglutinin (H) protein, which subsequently triggers the fusion (F) protein to mediate membrane merger and viral entry (Plemper et al., 2004). Beyond their role in infection, these receptors are targets for novel therapies, such as the antibody-drug conjugate enfortumab vedotin for Nectin-4-positive cancers and experimental entry inhibitors like AS-48 for measles treatment (Plemper et al., 2004; ASCO Daily News, 2020). Targeting these receptors or the viral proteins that bind to them is a key strategy for developing antivirals and oncolytic therapies (Muhlebach et al., 2011; BioWorld, 2024).
Inhibition of viral attachment, inhibition of membrane fusion, receptor blockade, and antibody-drug conjugate-mediated cytotoxicity.
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