Interleukin-8 homolog (vIL-8) is a chemokine encoded by the genome of Marek's disease virus. Chicken IL-8 (cIL8) is an important chemokine of chickens which plays a role in antiviral activity. To explore the relationship between vIL-8 and cIL8 can help to discern the function of vIL-8. In this study, the amino acid sequences of vIL-8 and cIL8 were aligned. The cIL8 gene was expressed in E. coli and the cIL8 fusion protein was obtained, after induction with IPTG. The protein was separated by SDS-PAGE and the band of interest was excised and minced for mouse immunization. An immunofluorescence test was used to detect vIL-8 expression in insect cells. The results showed that both vIL-8 and cIL8 were typical CXC chemokines in structure, and they had similar key amino acids, known to be important for receptor binding. The result of the immunofluorescence test showed that the mouse anti-cIL8 serum could react with vIL-8 expressed by insect cells. Therefore, vIL-8 shares common antigenic determinants with cIL8, and they may have a common receptor. This feature of vIL-8 suggests that it may participate in the immune evasion of the virus.
