Varicella-zoster virus entry receptors

The host cell entry receptors engaged by Varicella-zoster virus (VZV) glycoproteins constitute a diverse group of surface molecules that facilitate viral attachment, internalization, and membrane fusion (Arvin and Abendroth, 2021). Key members include the insulin-degrading enzyme (IDE), which interacts with viral glycoprotein E (gE) to promote infection and cell-to-cell spread (Li et al., 2006), and the cation-independent mannose 6-phosphate receptor (CI-MPR), which recognizes mannose 6-phosphate residues on several VZV glycoproteins (gB, gE, gH, gI) to mediate the entry of cell-free virus (Chen et al., 2004; Hambleton et al., 2007). Additionally, myelin-associated glycoprotein (MAG) serves as a receptor for glycoprotein B (gB), particularly in neural tissues, contributing to the virus's neurotropic nature (Suenaga et al., 2010). Initial viral tethering is typically achieved through interactions with heparan sulfate proteoglycans (HSPGs) (Zhu et al., 1995). These receptors are essential for the VZV life cycle and represent potential targets for antiviral therapy, although their critical roles in host physiology—such as metabolic regulation, lysosomal enzyme trafficking, and myelin maintenance—pose significant challenges for drug development (Li et al., 2010; Suenaga et al., 2010). Experimental inhibitors like bacitracin and mannose 6-phosphate have been used to study these interactions, but clinical treatments currently focus on viral proteins rather than host receptors (Li et al., 2006; Chen et al., 2004).

Other names

Varicella-zoster virus entry receptorsVZV entry receptorsHost cell receptors for VZVInsulin-degrading enzyme (IDE)Cation-independent mannose 6-phosphate receptor (CI-MPR)IGF2RMyelin-associated glycoprotein (MAG)Siglec-4Heparan sulfate proteoglycans (HSPGs)

Inhibition of viral attachment and entry by blocking glycoprotein-receptor interactions or preventing membrane fusion.