Fusion glycoprotein (F) of rinderpest virus: entire nucleotide sequence of the F mRNA, and several features of the F protein.

The full-length cDNA corresponding to the mRNA for the fusion protein of rinderpest virus (RV) was cloned and its complete nucleotide sequence was determined. The mRNA for the F protein was composed of 2359 nucleotides and contained a single large open reading frame which was capable of encoding 566 amino acids with a molecular weight (MW) of 58,929. The RV-F mRNA had a long noncoding region at the 5' end (586 bases) which was C-rich like the measles virus (MV)-F mRNA but they did not appear to be homologous with each other. Their secondary structure with long G-C stems suggested that they are easily folded. The coding region of RV-F mRNA was significantly homologous with that of MV-F; 74% of the nucleotides and 79.0% [corrected] of the amino acids were identical. The predicted RV-F protein had a basic amino acid region (104-108) which may be cleaved by protease to yield an activated form of F1,2. Three regions (1-19, 109-133, 418-513) were highly hydrophobic, and the N-terminal hydrophobic region of F1 or the positions of cysteines were significantly conserved compared with those of the other paramyxovirus F proteins. Three potential sites for glycosylation existed only in the F2 protein. Several features of the predicted RV-F protein were confirmed in polyacrylamide gel electrophoresis.