Zika virus precursor membrane protein (prM)

The Zika virus precursor membrane protein (prM) is a structural component essential for the assembly and maturation of the Zika virus, a flavivirus responsible for outbreaks linked to microcephaly and neurological disorders. In immature virions, prM forms heterodimers with the envelope (E) protein, creating trimeric spikes that project from the viral lipid membrane; the pr domain at the spike's apex covers the E protein's fusion loop, preventing premature fusion in low-pH environments like the Golgi apparatus. During maturation, host furin cleaves prM into the mature membrane (M) protein and a pr peptide, enabling the virus to adopt a smooth, infectious conformation capable of entering host cells via receptor-mediated endocytosis. Incomplete cleavage results in mosaic particles with mixed immature and mature features, potentially enhancing infectivity and evading host immunity. The derived M protein integrates into the mature virion membrane, where it may form oligomeric viroporin channels that facilitate early infection stages, such as entry or uncoating, particularly at acidic pH. As a therapeutic target, prM/M influences virus egress, stability, and host interaction, with inhibitors like rimantadine blocking M channel activity to reduce viremia in preclinical models.

Other names

pre-membrane proteinprecursor M proteinpre-envelope protein

Channel blockade of M protein viroporin activity during virus entry