Molecular cloning, characterization, and immunolocalization of two lactate dehydrogenase homologous genes from Taenia solium

• Published in: Parasitology research (1987) Vol. 109; no. 3; pp. 567 - 574
• Main Authors: Du, Wuying, Hu, Fengyu, Yang, Yabo, Hu, Dong, Hu, Xuchu, Yu, Xinbing, Xu, Jin, Dai, Jialin, Liao, Xinjiang, Huang, Jiang
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer-Verlag 01.09.2011; Springer; Springer Nature B.V
• Subjects: Amino acid sequence; Amino acids; Analysis; Animals; Antibodies, Helminth - blood; Antigenic determinants; Antigens; Biological and medical sciences; Biomedical and Life Sciences; Biomedicine; Blotting, Western; Cestode diseases; Cloning; Cloning, Molecular; Conserved sequence; Cross Reactions; Danio rerio; Dehydrogenases; Epitopes; Epitopes - immunology; Escherichia coli; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; General aspects; General aspects and techniques. Study of several systematic groups. Models; Genes; Genetic research; Humans; Immunodiagnosis; Immunology; Invertebrates; L-Lactate dehydrogenase; L-Lactate Dehydrogenase - analysis; L-Lactate Dehydrogenase - genetics; L-Lactate Dehydrogenase - immunology; Lactic acid; Localization; Lymphocytes B; Medical Microbiology; Microbiology; Nucleotide sequence; Original Paper; Physicochemical properties; Praziquantel; Rats; Rats, Sprague-Dawley; Schistosoma japonicum; Sequence Homology, Amino Acid; Sus scrofa; Swine; Taenia solium; Taenia solium - enzymology; Taenia solium - genetics; Tegument; Xenopus laevis; China; Artemether; Schistosoma Japonicum; Cysticercosis; Praziquantel; Gossypol; Gene; Helmintha; Plathelmintha; Parasite; Cestoda; Invertebrata; Molecular cloning; Taenia solium
• ISSN: 0932-0113; 1432-1955
• DOI: 10.1007/s00436-011-2285-8

Two novel genes encoding lactate dehydrogenase A (LDHA) and B (LDHB) homologues, respectively, were identified from the cDNA libraries of adult Taenia solium ( T. solium ). The two deduced amino acid sequences both show more than 50% identity to the homologues for Danio rerio , Xenopus laevis , Schistosoma japonicum , Sus scrofa , Homo sapiens , et al. The identity of the amino acid sequence between Ts LDHA and Ts LDHB is 57.4%, and that of the nucleotide sequence is 61.5%. Recombinant Ts LDHA homologue (r Ts LDHA) and Ts LDHB homologue (r Ts LDHB) were expressed in Escherichia coli BL21/DE3 and purified. Though there were some differences in the sequence, the two LDH isozyme homologues show similarity in the conserved LDH domain, topological structure, primary immunological traits, localization on the tegument of T. solium adult, and partial physicochemical properties. The linear B-cell epitope analysis of Ts LDHA and Ts LDHB discovered a Ts LDHA specific epitope. The purified r Ts LDHA and r Ts LDHB could be recognized by rat immuno-sera, serum from swine, or a patient infected with T. solium , respectively, but Western blot analysis showed cross-reactions, not only between these two LDH members but also with other common human tapeworms or helminths. The results suggested that the two LDH homologues are similar in the characteristics of LDH family, and they are not specific antigens for immunodiagnosis.