Sphingolipid biosynthesis induces a conformational change in the murine norovirus receptor and facilitates viral infection.

ABSTRACT: Cellular susceptibility to viral infections is in part determined by the presence of a host cellular receptor. Here we use murine norovirus as a model to uncover an unappreciated connection between an intracellular lipid biosynthetic enzyme and a receptor conformation that is permissive for viral infection. The serine palmitoyltransferase complex is required for de novo sphingolipid biosynthesis and we find that its absence impairs the ability of murine norovirus to bind and enter cells. Although the serine palmitoyltransferase complex is dispensable for the surface expression of the norovirus receptor, CD300lf, serine palmitoyltransferase activity is required for CD300lf to adopt a conformation permissive for viral binding. Addition of extracellular ceramide to serine palmitoyltransferase

SUBMITTER: Orchard RC 

PROVIDER: S-EPMC6158067 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature