Skip to main content


Fig. 1 | Virology Journal

Fig. 1

From: The pH stability of foot-and-mouth disease virus

Fig. 1

The location in FMDV capsid of amino acid residues found to be substituted in Table 1. a, b and c Outside view of a respective pentamer model of C-S8c1, A22 Iraq and O1BFS (PDB: 1FMD, 4GH4 and 1BBT). The red amino acid residues are ones which are marked with ‘a’ in Table 1 and the black ones are those residues which are marked with ‘b’ in Table 1. The VP1 is green; VP2 is purple; VP3 is blue; VP4 is orange. According to the gene sequence of FMDV C-S8c1 and A22 Iraq, residues D115, A116, A118 and A123 in Table 1 are labeled as D116, A117, A119 and A124 in panel (a), and residues A3 and D133 are labeled as T3 and T133 in panel (b). d Outside view of schematic structure of part FMDV capsid. The VP1 is green; VP2 is purple; VP3 is blue (five-fold axis, pentagon; three-fold axis, triangle; two-fold axis, diamond). e and f Outside view of six protomers around a three-fold axis and two pentamers model of C-S8c1 capsid. The color of VP1, VP2, VP3, and VP4 are the same as those in panel a, b, and c. Three-fold axis is triangle; two-fold axis is diamond; five-fold axis is pentagon; intersection of VP1, VP2, and VP3 is four point star. All red amino acid residues in panel a, b, and c are displayed in panel e and f, respectively. Those red residues are included in a yellow quadrangle region in which the three-fold axis, two-fold axis and the intersections of three capsid proteins (VP1, VP2, and VP3) act as the four vertexes

Back to article page