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Measles virus receptors are host cell surface proteins that facilitate the attachment and entry of the measles virus (MeV) into human cells. The primary receptors for wild-type MeV are Signaling Lymphocytic Activation Molecule Family Member 1 (SLAMF1, also known as CD150) and Nectin-4 (PVRL4) (Tatsuo et al., 2000, Nature; Muhlebach et al., 2011, Nature). SLAMF1 is predominantly expressed on immune cells such as T cells, B cells, and dendritic cells, mediating the initial infection and systemic spread (Noyce and Richardson, 2012, Rev. Med. Virol.). Nectin-4 is an adherens junction protein expressed on the basolateral surface of epithelial cells, which the virus uses to exit the host and spread via respiratory droplets (Muhlebach et al., 2011, Nature). While vaccine strains can also utilize CD46 (Membrane Cofactor Protein), wild-type virus primarily relies on SLAMF1 and Nectin-4 (Naniche et al., 1993, J. Virol.). These receptors are significant not only for understanding viral pathogenesis but also as therapeutic targets; for instance, Nectin-4 is a validated target for antibody-drug conjugates like enfortumab vedotin in oncology (FDA, Padcev Prescribing Information).
Antibody-drug conjugate (ADC) targeting Nectin-4 to deliver the microtubule-disrupting agent monomethyl auristatin E (MMAE); blockade of viral hemagglutinin (H) protein binding to host receptors to prevent viral entry.
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