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The Parvovirus B19 VP1u receptor (VP1uR) is a critical cellular component required for the entry of human parvovirus B19 (B19V) into permissive host cells, specifically erythroid progenitor cells (EPCs) (Leisi et al., 2013). While the virus initially attaches to the cell surface via globoside (P antigen), the subsequent internalization process is strictly dependent on the high-affinity interaction between the unique N-terminal region of the viral VP1 capsid protein (VP1u) and the VP1uR (Leisi et al., 2016). This receptor is highly restricted to the erythroid lineage, explaining the narrow tropism of B19V and its specific impact on hematopoiesis. Although Axl tyrosine kinase was previously proposed as the identity of VP1uR, recent studies suggest that the functional receptor on EPCs may be a distinct, yet-to-be-fully-characterized protein (Bieri et al., 2021). In clinical contexts, the B19V-VP1uR interaction is the primary driver of viral pathogenesis, leading to the destruction of red blood cell precursors and resulting in diseases such as erythema infectiosum, transient aplastic crisis, and fetal hydrops. Therapeutic development focuses on blocking this interaction using VP1u-mimetic peptides or neutralizing monoclonal antibodies to prevent viral entry and protect vulnerable patient populations (Kaikkonen et al., 2016).
Competitive inhibition of viral attachment and internalization by blocking the interaction between the viral VP1u domain and the cellular VP1u receptor.
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