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The Feline infectious peritonitis virus (FIPV) membrane (M) glycoprotein is a critical structural component of the viral envelope and is the most abundant protein in the virion (UniProt P0C6T5). It plays a central role in viral morphogenesis by coordinating the assembly of viral particles through interactions with the nucleocapsid (N) protein and the spike (S) glycoprotein at the endoplasmic reticulum-Golgi intermediate compartment (Fehr & Perlman, 2015). Beyond its structural role, the M protein is involved in the packaging of the viral RNA genome into the budding particles. In the context of Feline Infectious Peritonitis (FIP), a fatal systemic disease in cats, the M protein serves as a significant antigen for the host immune response and is a target for diagnostic assays and vaccine research (Addie et al., 2009). While current frontline therapeutics for FIP primarily target the viral polymerase or protease, the M protein remains a subject of interest for strategies aimed at disrupting viral assembly. However, vaccine development involving FIPV structural proteins must carefully navigate the risk of antibody-dependent enhancement (ADE), which can exacerbate the disease (Hohdatsu et al., 1998).
Inhibition of viral assembly and budding
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