The cysteine protease TsCL-1 gene of Cysticercus cellulosae was amplified from the total RNA of C.cellulosae by RT-PCR.Then the fusion expression vector pPIC9K-TsCL-1 was constructed by inserting the amplified TsCL-1 gene into pPIC9K,and was transformed to GS115 by electroporation.Multicopy recombinant strains were screened by G418 and induced by methanol.SDS-PAGE was used to analyze expression product.The results showed that the gene shared 99.8% and 100% identity at the nucleotide and amino acid levels to the ones available in GenBank,and 76.3% amino acid similarity to cathepsin of Fasciola hepatica and Fasciola gigantica,respectively.The recombinant pTsCL-1 was expressed successfully in Pichia pastoris,and was approximately 42 ku in molecular mass.Western-blot analysis showed that the expressed recombinant protein had reactogenicity.

Genomic DNA was extracted from the skin tissue of suspected capripox sheep in Jingtai, Gansu Province, and the glycoprotein-encoding orf118 gene was cloned by PCR. Comparison shows that the length of open reading frame of glycoprotein-encoding orf118 gene is 516 bp, coding for a 171-amino acid protein with molecular weight of approximate 19 500, and its nucleotide component showed a serious imbalance with 72.48% of A+T and 27.52%of G+C. The homology of nucleotide and deduced amino acid sequence between sheeppox virus ,Gansu strain and sheeppox virus TU-V02127 strain is 99.8% and 100%, respectively. orf118 of the sheeppox virus, Gansu strain shares 96.5% and 94.8% of identity with Lumpy skin disease virus and goatpox virus G20-LKV strain at a nucleotide level. Structural prediction of the deduced orf118 protein indicates that the orf118 antigen is a secretory glycoprotein with two N-linked glycosylation sites and one trans-membrane domain. Together with above results suggest that the orf118 glycoprotein is completely conserved among sheeppox field strains and has potential value for vaccine and diagnosis.