Effect of the ionophore monensin on herpes simplex virus type 1-induced cell fusion, glycoprotein synthesis, and virion infectivity.
The ionophore monensin inhibited the formation of mature, fully glycosylated glycoproteins gB, gC, and gD during herpes simplex virus type 1 infection of human embryonic lung cells. Underglycosylated forms, including the apparent high-mannose precursor forms of the major glycoproteins, appeared. Monensin inhibited virus-induced cell fusion. Infectious virions produced in the presence of monensin appeared to contain predominantly underglycosylated glycoproteins.
D002459:Cell Fusion / Q000187:drug effects; D002478:Cells, Cultured; D004622:Embryo, Mammalian; D005663:Furans / Q000494:pharmacology*; D006023:Glycoproteins / Q000096:biosynthesis; D006801:Humans; D008168:Lung; D008985:Monensin / Q000494:pharmacology*; D018139:Simplexvirus / Q000187:drug effects*; D014764:Viral Proteins / Q000096:biosynthesis
D005663:Furans; D006023:Glycoproteins; D014764:Viral Proteins; D008985:Monensin