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The host cell receptors for attenuated measles, mumps, and rubella viruses are a collection of surface molecules that mediate the entry of vaccine-strain viruses into host cells. For the attenuated measles virus (Edmonston strain), the primary receptor is Membrane cofactor protein (CD46), which is a regulator of the complement system (Dorig et al., 1993). This is distinct from wild-type measles virus, which uses Signaling lymphocytic activation molecule family member 1 (SLAMF1) and Nectin-4. Mumps virus utilizes sialic acid residues, particularly alpha-2,3-linked sialic acids, as receptors for its hemagglutinin-neuraminidase protein (Kubota et al., 2016). Rubella virus has been identified to use Myelin oligodendrocyte glycoprotein (MOG) as a key entry receptor, which is significant given the virus's potential for neurological involvement (Cong et al., 2011). These receptors are critical for the efficacy of the MMR vaccine, as they allow the attenuated viruses to infect cells and stimulate a robust, long-lasting immune response. Understanding these interactions is essential for evaluating vaccine safety, especially in patients with underlying immunological or neurological conditions.
The attenuated viruses in the MMR vaccine bind to these specific host receptors (CD46 for measles, sialic acid for mumps, and MOG for rubella) to trigger membrane fusion and viral entry, leading to a controlled infection that stimulates long-term adaptive immunity.
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