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The Feline infectious peritonitis virus (FIPV) membrane protein, historically referred to as the small integral membrane glycoprotein, is the most abundant structural protein of the viral envelope [1, 4]. It is a triple-spanning membrane protein that plays a central role in virion morphogenesis by coordinating the assembly of other structural proteins, including the Spike (S), Envelope (E), and Nucleocapsid (N) proteins [7, 11]. In the pathogenesis of FIP, the M protein is a key immunological target; monoclonal antibodies like FK50-4 have been demonstrated to neutralize the virus and prevent infection in feline macrophages, the primary host cells for FIPV [1]. Unlike the Spike protein, which is often implicated in antibody-dependent enhancement (ADE), the M protein contains conserved epitopes that are candidates for safer vaccine designs and therapeutic antibodies [2, 8]. While research into small-molecule inhibitors for the M protein is ongoing, it remains a critical target for disrupting the viral life cycle and preventing the fatal progression of feline infectious peritonitis [4, 16].
Neutralization of viral entry and replication; interference with virion assembly and budding.
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