Structure oftheFMDV translation initiation site andofthestructural proteins

A cDNAcloneofFootandMouthDisease Virus(FMDV), strainCl,hasbeen sequenced. Thelimits ofthestructural genesweredefined bycomparison with theavailable protein data.Weidentified twopotential translation initiationsitesfortheviralpolyprotein separated by84nucleotides. Wesuggest thatthesetwoinitiation sitescouldbeusedtoexpresstwoproteins differingonlyattheN-termini, P16andP20a.Thismodelissupported bythefact thatantiserum against a bacterially synthesized polypeptide corresponding totheanterior regionofthepolyprotein precipitates specifically bothP16 andP20a.Comparison oftheClsequence withtwootherserotypes, 01KandA10 revealed variability inthemajorimmunogenic structural protein, VP1,and alsointwoothercapsidproteins, VP2andVP3.P16/P20a, VP4,andtheN-terminalpartoftheprecursor ofthenonstructural genes,P52,areratherconservedbetween thedifferent FMDVstrains.