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The host cell entry receptors for mumps, rubella, and varicella-zoster virus (VZV) vaccine strains are a collection of distinct cellular molecules that facilitate the infection of host cells by live-attenuated vaccine viruses. For the mumps virus (MuV) vaccine strains like Jeryl Lynn, the primary receptor is sialic acid, specifically alpha-2,3-linked sialic acid, which is ubiquitously expressed on cell surface glycoproteins and glycolipids (Kubota et al., 2016, PNAS). The rubella virus (RuV) vaccine strain RA 27/3 utilizes myelin oligodendrocyte glycoprotein (MOG) and cell adhesion molecule 1 (CADM1) as functional receptors for entry into host cells (Cong et al., 2011, Nature Medicine; Kono et al., 2020, Journal of Virology). For VZV vaccine strains such as the Oka strain, entry is mediated by the insulin-degrading enzyme (IDE), which acts as a receptor for viral glycoprotein gE, and the mannose 6-phosphate receptor (MPR), which is involved in viral trafficking (Li et al., 2006, Science; Chen et al., 2004, Science). These receptors are essential for the biological activity of vaccines like MMR II and Varivax, as they determine the tissue tropism and the ability of the attenuated viruses to replicate sufficiently to induce immunity. While these molecules serve normal physiological roles—such as proteolysis for IDE or myelin maintenance for MOG—their exploitation by vaccine strains is the basis for generating protective immune responses against mumps, rubella, and chickenpox.
Live-attenuated vaccine viruses bind to these specific host cell surface receptors to facilitate viral entry and subsequent replication, which triggers the host's adaptive immune response.
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