Genetic characterization of the cell-adapted PanAsia strain of foot-and-mouth disease virus O/Fujian/CHA/5/99 isolated from swine

Abstract

Abstract Background According to Office International Des Epizooties (OIE) Bulletin, the PanAsia strain of Foot-and-Mouth Disease Virus (FMDV) was invaded into the People's Republic of China in May 1999. It was confirmed that the outbreaks occurred in Tibet, Hainan and Fujian provinces. In total, 1280 susceptible animals (68 cattle, 1212 swine) were destroyed for the epidemic control. To investigate the distinct biological properties, we performed plaque assay, estimated the pathogenicity in suckling mice and determined the complete genomic sequence of FMDV swine-isolated O/Fujian/CHA/5/99 strain. In addition, a molecular modeling was carried out with the external capsid proteins. Results The pathogenicity study showed that O/Fujian/CHA/5/99 had high virulence with respect to infection in 3-day-old suckling-mice (LD50 = 10-8.3), compared to O/Tibet/CHA/1/99 (LD50 = 10-7.0) which isolated from bovine. The plaque assay was distinguishable between O/Fujian/CHA/5/99 and O/Tibet/CHA/1/99 by their plaque phenotypes. O/Fujian/CHA/5/99 formed large plaque while O/Tibet/CHA/1/99 formed small plaque. The 8,172 nucleotides (nt) of O/Fujian/CHA/5/99 was sequenced, and a phylogenetic tree was generated from the complete nucleotide sequences of VP1 compared with other FMDV reference strains. The identity data showed that O/Fujian/CHA/5/99 is closely related to O/AS/SKR/2002 (94.1% similarity). Based on multiple sequence alignments, comparison of sequences showed that the characteristic nucleotide/amino acid mutations were found in the whole genome of O/Fujian/CHA/5/99. Conclusion Our finding suggested that C275T substitution in IRES of O/Fujian/CHA/5/99 may induce the stability of domain 3 for the whole element function. The structure prediction indicated that most of 14 amino acid substitutions are fixed in the capsid of O/Fujian/CHA/5/99 around B-C loop and E-F loop of VP2 (antigenic site 2), and G-H loop of VP1 (antigenic site 1), respectively. These results implicated that these substitutions close to heparin binding sites (E136G in VP2, A174 S in VP3) and at antigenic site 1 (T142A, A152T and Q153P in VP1) may influence plaque size and the pathogenicity to suckling mice. The potential of genetic characterization would be useful for microevolution and viral pathogenesis of FMDV in the further study.