White spot syndrome virus (WSSV）is one of the major pathogen of shrimp culture with a wide host range and high mortality rate. Since it first appeared in the 1990s, WSSV has spread around the world rapidly, caused large damage to shrimp aquaculture and serious threat to world water environment. WSSV with a low homology to the known virus has been classified into a new virus family. So it is difficult to infer the molecular mechanism of WSSV systemic infection from the known viruses. Since the shrimp cell line has not been established yet, it is difficult to study the structural proteins of WSSV and its infection mechanism using conventional methods. To date, there is no efficient method to protect shrimp from WSSV despite of more progress on the study of genome and proteome of WSSV. In this work, phage display technology was used to probe into a new way to study the structural proteins of WSSV. VP28 is one of the major envelope proteins of WSSV and may paly a key role in WSSV infectivity. In this study, using phage display technology, a single-chain fragment variable (scFv) antibody library displayed on phages was constructed using spleen from the mice immunized with VP28 expressed in Escherichia coli. After several rounds of panning, six scFv antibodies with different CDR3 in their heavy chain specifically binding to the epitopes in the N-terminal, middle and C-terminal regions of VP28 respectively were isolated from the library. Four of the scFvs recognize linear epitopes and the other two recognize conformational epitopes. Using these scFv antibodies as tools, the epitopes in VP28 were located on the envelope of the virion by immuno-electron microscopy and some of the epitopes were located in the inner of the trimer of VP28. Neutralization assay with these antibodies in vitro and in vivo showed that none of the scFvs could inhibit or delay WSSV infectivity. The result suggests that these epitopes may not be the attachment site of WSSV to host cell receptor. At the same time, a recombinant protein VP28 fused with enhanced green fluorescent protein (EGFP) was constructed and expressed in E. coli. Using EGFP as reporter, the interaction between VP28 and host cell was investigated by flow cytometry and fluorescent microscopy. It is a pity that the result indicated that no direct interaction between VP28 and host cell was appeared, which is different from that of other researcher. After the work on VP28 in our lab, we think that further study on the function and mechanism of VP28 in infection is very necessary. In order to study the function of more structural proteins of WSSV, a scFv antibody phage display library was constructed using spleen from mice immunized with denatured WSSV. After investigation of several panning methods, the efficient methods to generate more different scFvs binding to different epitopes of WSSV were established and six scFvs specifically against WSSV were isolated and characterized. One of the scFvs recognizes a linear epitope and can be used in Western blot assay. The location of the epitopes bound by the isolated scFvs on WSSV was performed by mmuno-electron microscopy. This study provides a new strategy to obtain more different antibodies specifically binding to WSSV. The isolated scFv P75E8 recognizes a linear epitope in VP28. In order to establish a high throughout method to identify the epitopes bound by scFvs using phage display technology, two methods were adopted to identify the epitope bound by scFv P75E8: 1) using conventional method, ELISA assay of binding between P75E8 with several truncated VP28 proteins to determine the epitope; 2) using phage display technology, a panning against a phage display random decapeptide library was performed using purified P75E8 as an immobilized target. The epitope was determined with a amino acid sequence: SDAQMKEEDA using method 1). But we could not infer the epitope recognized by P75E8 using method 2) despite a lot of positive clone were isolated. Further study indicated that P75E8 immobilized randomly lost the ability to bind to VP28. So it is very important to establish efficient way to directionally limmobilize scFv before panning. The work lays the groundwork for further research on epitope recognized by scFv.