Clinical Immunology and Infectious Diseases

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Measles Virus Scholarly Peer-review Journal

The hemagglutinin (H) protein of measles virus (MeV) interacts with a cellular receptor which constitutes the initial stage of infection. Binding of H to the present host cell receptor subsequently triggers the F protein to activate fusion between virus and host plasma membranes. The look for MeV receptors began with vaccine/laboratory virus strains and evolved to more relevant receptors employed by wild-type MeV. Vaccine or laboratory strains of measles virus are adapted to grow in common cell lines like Vero and HeLa cells, and were found to use membrane cofactor protein (CD46) as a receptor. CD46 may be a regulator that normally prevents cells from complement-mediated self-destruction, and is found on the surface of all human cells, with the exception of erythrocytes. Mutations within the H protein, which occur during adaptation and permit the virus to use CD46 as a receptor, are identified. Wild-type isolates of measles virus cannot use the CD46 receptor. However, both vaccine/laboratory and wild-type strains can use an immune cell receptor called signaling lymphocyte activation molecule loved one 1 (SLAMF1; also called CD150) and a recently discovered epithelial receptor referred to as Nectin-4. SLAMF1 is found on activated B, T, dendritic, and monocyte cells, and is that the initial target for infections by measles virus. Nectin-4 is an adherens junction protein found at the basal surfaces of the many polarized epithelial cells, including those of the airways. it's also over-expressed on the apical and basal surfaces of the many adenocarcinomas, and may be a cancer marker for metastasis and tumor survival. Nectin-4 may be a secondary exit receptor which allows measles virus to duplicate and amplify within the airways, where the virus is expelled from the body in aerosol droplets.

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