Posttranslational processing of Uukuniemi virus glycoproteins G1 and G2.

Uukuniemi virus, which matures specifically in the Golgi complex, contains two species of envelope glycoproteins, G1 (Mr, 70,000) and G2 (Mr, 65,000). These are translated as a polyprotein, p110, from an mRNA which is complementary to the medium-sized segment of the virion RNAs. By synchronized initiation of protein synthesis and pulse-labeling, it was shown that glycoprotein G1 is amino terminal in precursor protein p110. Apparently, the nonglycosylated forms of these proteins (Mr, 54,000 to 57,000), synthesized in the presence of tunicamycin, comigrate in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, because a similar-sized protein could be isolated by immunoprecipitation with monoclonal antibodies directed against either G1 or G2. The G1 protein, which in the virion contains exclusively endoglycosidase H (endo H)-resistant glycans, was converted to the endo H-resistant form in a half time of about 45 min. The G2 protein, which in the virion has a heterogeneous glycosylation pattern as revealed by endo H digestion, attained this partial endo H resistance only after 90 to 150 min of chase. The transport time of Uukuniemi virus glycoproteins from the endoplasmic reticulum to the Golgi complex was considerably longer than that for alpha and rhabdovirus glycoproteins. Determination of the transport time of G1 and G2 to extracellular virions revealed that G1 is incorporated into mature virions about 10 min faster than G2, suggesting that G1 and G2 are transported with different kinetics to the site of virus maturation.