Abstract: Field isolates of foot-and-mouth disease virus (FMDV) are believed to use integrins as cellular receptors for virus internalization in vivo. In this study, we first cloned and sequenced the cDNA encoding porcine integrin β8 from the tongue keratinocytes of pig infected experimentally with FMDV. The 2 304 bp cDNA of porcine integrin β8 encodes a polypeptide of 767 amino acids consisting of a 42-residue putative signal peptide, a 637-residue ectodomain, a 30residue transmembrane domain, and a 58-residue cytoplasmic domain. The ectodomain contains 7 potential N-linked glycosylation sites（NXT/NXS）and 49 cysteine residues. The nucleotide sequence similarity of integrin β8 between pig and cattle, human, dog, rhesus monkey, house mouse, Norway rat are 94.3%，91.4%，91.7%，91.4%，83.5%，83.5%, and the amino acid sequence similarity are 95.0%，91.8%，92.8%，91.5%，84.0%，84.8%,respectively. The secondary structure of porcine β8 contains α-helix, β-sheet, β-turn and coil regions.The hydropathic analysis of the polypeptide revealed two hydrophobic domains,the signal peptide(1-42aa) and transmembrane domain(680-709aa). This study will lay a foundation for understanding the interactions of FMDV with receptors.