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The Zika virus pre-membrane protein (prM) is a structural protein essential for the assembly and maturation of the Zika virus (ZIKV) [1]. It functions primarily as a chaperone for the Envelope (E) protein, forming a prM-E heterodimer that prevents the E protein from undergoing premature fusion in the acidic environment of the host cell's secretory pathway [2]. During the maturation process in the trans-Golgi network, the host protease furin cleaves prM into a 'pr' peptide and a mature 'M' protein, which triggers a conformational change that renders the virus infectious [3]. As a key surface-exposed component of the immature virion, prM is a major focus in vaccine design, typically utilized alongside the E protein to induce protective immune responses [4]. However, prM-specific antibodies are frequently non-neutralizing and have been implicated in antibody-dependent enhancement (ADE), a phenomenon where they may increase the severity of infection by facilitating viral entry into immune cells, particularly in individuals previously exposed to Dengue virus [5, 6]. Consequently, while prM is a vital therapeutic target, its role in ADE presents a significant challenge for the development of safe and effective Zika vaccines and therapeutics [6].
Induction of neutralizing antibodies, inhibition of viral maturation, and prevention of viral entry into host cells.
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