Human Norovirus (HuNoV) is a single stranded (+)RNA virus and the leading cause of non-bacterial diarrhea in the world – causing 685 million infections annually. As HuNoV is unable to be cultured in the lab, Murine Norovirus (MNV) is the only model for investigate norovirus pathogenesis. The intracellular replication of Noroviruses - and arguably all (+)RNA viruses - is dependent on host resources including proteins, metabolites and lipids. (+)RNA viruses especially commandeer organelle membranes to construct viral Replication Complexes (RC), which allow efficient replication by creating a sheltered environment in which replication can occur. Here we investigate the host lipid utilization by MNV, and identify the key host proteins that facilitate the viral-induced subversion of lipid biosynthesis pathways. In particular, we focus on the host lipid Phosphotidylinositol 4-Phosphate (PI4P) and its contribution to efficient virus replication. PI4P is normally present in plasma and organelle membranes, and has been shown to be utilized in replication of other (+)RNA viruses. Previously we have shown that PI4P and PI4P kinases localize to sites of MNV replication. Here we demonstrate that PI4P is upregulated during MNV infection through the action of PI4KIII3α. We have interrogated this interaction using chemical inhibition of PI4P kinases, reconfirming colocalization between PI4P and MNV NS4, as well as showing a reduction in viral protein and RNA when PI4KIII3α is inhibited. We hypothesize that identification of key host components that facilitate virus replication will enable the development of compounds with antiviral potential.