Characterization of emY162 encoding an immunogenic protein cloned from an adult worm-specific cDNA library of Echinococcus multilocularis

• Published in: Biochimica et biophysica acta Vol. 1780; no. 1; pp. 1 - 6
• Main Authors: Katoh, Yoshinobu, Kouguchi, Hirokazu, Matsumoto, Jun, Goto, Akiko, Suzuki, Tomohiro, Oku, Yuzaburo, Yagi, Kinpei
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 2008
• Subjects: Adult worm; Amino Acid Sequence; Animals; Base Sequence; Blotting, Western; cDNA library; Dogs; Echinococcus multilocularis; Echinococcus multilocularis - genetics; Echinococcus multilocularis - metabolism; emY162 cDNA; Gene Library; Helminth Proteins - genetics; Helminth Proteins - immunology; Helminth Proteins - metabolism; Immune Sera - immunology; Immunogenic protein; Immunoglobulin G - immunology; Molecular Sequence Data; Recombinant EMY162 antigen; Recombinant Proteins - immunology; Recombinant Proteins - metabolism; Sequence Alignment; Sequence Analysis, DNA; Echinococcus multilocularis; Adult worm; Recombinant EMY162 antigen; Immunogenic protein; cDNA library; emY162 cDNA
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2007.08.020

A cDNA library based on mRNA from adult worms of Echinococcus multilocularis was constructed. One cDNA clone, emY162, was isolated from this cDNA library. The putative protein from emY162 cDNA consists of 153 amino acids and has a predicted molecular weight of 17.0 kDa. The amino acid sequences of EMY162 are predicted to be a hydrophobic N-terminus conserving a secretory signal, and a hydrophobic C-terminus encoding a transmembrane domain or glycosyl-phosphatylinositol membrane anchor, and to have single fibronectin type III-like domain. In addition, it was shown that the emY162 gene (1738 bp) in the E. multilocularis genome DNA consists of three exons and two introns, and that emY162 is expressed in all four stages (protoscoleces, cultured metacestodes, immature adult worms and mature adult worms). Moreover, immunity to recombinant EMY162, which comprises the fibronectin type III-like domain on the EMY162 protein, was examined. Immune responses to the recombinant EMY162 were studied by using serum from dogs infected with E. multilocularis. Strong IgG immune responses were detected in Western blots.