Identification of a novel gene product expressed by Trichinella spiralis that binds antiserum to Sp2/0 myeloma cells

• Published in: Veterinary parasitology 2013-05, Vol.194 (2-4), p.183-185
• Main Authors: Duan, Lingxin, Li, Jianhua, Cheng, Boqi, Lv, Qiang, Gong, Peng-tao, Su, Li-bo, Cai, Yanan, Zhang, Xichen
• Format: Article
• Language: English
• Subjects: amino acids; Animals; antibodies; Antigens, Helminth - genetics; Antigens, Helminth - immunology; antiserum; bacteriophages; Binding Sites, Antibody - genetics; Binding Sites, Antibody - immunology; Bioinformatics; Cancer Vaccines - genetics; cDNA libraries; cDNA library; Cell Line, Tumor; clones; complementary DNA; Computational Biology; computer software; Epitope Mapping; epitopes; Epitopes - genetics; Epitopes - immunology; Gene Library; genes; Helminth Proteins - genetics; Helminth Proteins - immunology; Immune Sera - immunology; Larva - genetics; Mice; Mice, Inbred BALB C; Multiple Myeloma - immunology; Multiple Myeloma - pathology; muscle larvae; myeloma; open reading frames; proteins; RNA; RNA, Helminth - genetics; Sp2/0 myeloma cell; systems analysis; Trichinella spiralis; Trichinella spiralis - genetics; Trichinella spiralis - immunology; Tumor Suppressor Proteins - genetics; Tumor Suppressor Proteins - immunology; Ulmus; vaccines
• ISSN: 0304-4017; 1873-2550
• DOI: 10.1016/j.vetpar.2013.01.051

To obtain novel antigen genes for use as an anti-tumor vaccine, a Trichinella spiralis cDNA expression library was constructed from muscle larvae RNA and screened with sera from Balb/C mice injected with Sp2/0 myeloma cells. One positive clone was obtained after three rounds of immunoscreening of the cDNA expression library and was subsequently excised in vivo using the ExAssist helper phage with SOLR strain. A full-length gene was amplified using 5′-RACE technology and analyzed by BLAST, Protein Analysis System of ELM, and DNAStar Software. The sequencing results showed that the fragment was 569bp in length and contained an open reading frame. It was predicted that the full-length gene encoded 136 amino acids. This gene, TS2, contained four putative N-Arg dibasic convertase (nardilysine) cleavage sites, one peptide C-terminal amidation site, and one glycosaminoglycan attachment site. Six antibody epitopes were predicted by bioinformatic analysis.