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Parvovirus B19 capsid protein VP2 is the major structural component of the B19 virus (B19V), making up approximately 95% of the viral capsid [5, 7]. It plays a pivotal role in the viral life cycle by mediating attachment to the primary host cell receptor, globoside (P antigen), which is predominantly expressed on erythroid progenitor cells [2, 6]. This interaction is a prerequisite for viral entry and the subsequent destruction of red blood cell precursors, leading to clinical conditions such as erythema infectiosum (fifth disease), transient aplastic crisis, and hydrops fetalis [2, 7, 9]. VP2 is the primary target for neutralizing antibodies, making it a central focus for diagnostic assays and the development of virus-like particle (VLP) vaccines [5, 9]. Clinically, intravenous immunoglobulin (IVIG) is administered to provide passive immunity by delivering anti-VP2 antibodies to patients with persistent infections [7]. Additionally, research has highlighted the potential of recombinant VP2 to inhibit hematopoiesis, suggesting its possible application as a therapeutic agent for myeloproliferative disorders like polycythemia vera [1]. However, targeting or utilizing VP2 carries risks, including the potential for severe anemia or the formation of immune complexes that contribute to post-infection arthropathy [7, 9].
Neutralization of viral entry and inhibition of receptor binding; induction of protective humoral immunity; inhibition of hematopoietic progenitor cell proliferation.
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