Structural, biochemical and electrostatic basis of serotype specificity inbovine enteroviruses

We have performed immunostructural analyses of three closely related picorn aviruses in order to gain understanding of the biochemical and structural b asis of serotype specificity. We carried out sequence alignments of the cap sid regions of three bovine enterovirus strains: VG-5-27 and M-4 from serot ype 1 and PS-87 from serotype 2. Using our knowledge of the three dimension al and antigenic structure of strain VG-5-27 and the high levels of sequenc e identity between the strains, we have calculated the structures and solve nt-accessible electrostatic potentials of the epitopes of all three viruses . We have demonstrated the viability of the molecular models of the epitope s of the M-4 and PS-87 strains. In each of the strains, we have explained t he serotype specificities in terms of specific physical and chemical proper ties, and identified individual residues which are pivotal in determination of antibody recognition. These changes are in agreement with the known cro ss-reactivity of peptide and antiviral sera, showing that it is possible to derive structures for short variable sections of proteins of high sequence identity using molecular modelling which are significant in terms of biolo gical function. We believe this study to be a novel approach in the analysi s of virus serotype specificity.