Glycoprotein C

Lymphocytic choriomeningitis virus (LCMV) is a spherical enveloped virus with an RNA genome consisting of two negative single-stranded RNA segments, the large (L) strand and the small (S) strand. The L strand encodes the virus polymerase (L) and a small zinc finger motif protein (Z); the smaller (S) segment encodes the two main structural proteins: virus nucleoprotein (NP) and glycoprotein (GP) precursor (GPC). The GP of LCMV serves as virus attachment protein to its receptor on host cells and is a key determinant for cell tropism, pathogenesis, and epidemiology of the virus. The GP undergoes post-translational cleavage and results in the synthesis of two mature virion glycoproteins, GP-1 (40 to 46 kDa) and GP-2 (35 kDa). The spikes present on the virion envelope are dictated by tetramer formation of GP-1 and GP-2. The peripheral GP-1 is implicated in receptor binding, and the transmembrane GP-2 is structurally similar to the fusion active membrane proximal portions of the glycoproteins of other enveloped viruses.