The Marburg virus surface protein GP is phosphorylated at its ectodomain.

Marburg virus, a filovirus, contains only one transmembrane protein (GP) which is responsible for receptor recognition on target cells. GP, a type I membrane protein of approximately 220 kDa, is acylated and highly glycosylated carrying N- and O-linked sugar side chains. GP is transported through the exocytotic pathway toward the plasma membrane where budding of virions takes place. In the trans-Golgi network, GP is proteolytically activated by the prohormone convertase furin into two subunits GP(1) and GP(2). In the present paper, we provide evidence that GP undergoes an additional posttranslational modification; it is phosphorylated at its ectodomain. Phosphorylation takes place at serine residues between amino acid 260 and 273. The respective serines are located in conserved recognition sites for luminal protein kinases (protein kinase CK II and Golgi casein kinase). Consistent with this data, it was found that GP was phosphorylated in the Golgi apparatus of the expressing HeLa cells before cleavage of the molecule. GP is the first example of a viral glycoprotein with a phosphorylated ectodomain.