The study identifies two potential translation initiation sites for the FMDV polyprotein and highlights structural protein variability across serotypes.
May inform FMDV isoform modeling; leaves open functional roles and vaccine implications pending in vivo validation.
A cDNA clone of Foot and Mouth Diseases Virus (FMDV), strain C1, has been sequenced. The limits of the structural genes were defined by comparison with the available protein data. We identified two potential translation initiation sites for the viral polyprotein separated by 84 nucleotides. We suggest that these two initiation sites could be used to express two proteins differing only at the N-terminal, P16 and P20a. This model is supported by the fact that antiserum against a bacterially synthesized polypeptide corresponding to the anterior region of the polyprotein precipitates specifically both P16 and P20a. Comparison of the C1 sequence with two other serotypes, O1K and A10 revealed variability in the major immunogenic structural protein, VP1, and also in two other capsid proteins, VP2 and VP3. P16/P20a, VP4, and the N-terminal part of the precursor of the nonstructural genes, P52, are rather conserved between the different FMDV strains.
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Beck et al. (1983) studied this question.
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