An Eimeria vaccine candidate appears to be lactate dehydrogenase; characterization and comparative analysis

• Published in: Parasitology 2004-06, Vol.128 (6), p.603-616
• Main Authors: SCHAAP, D., ARTS, G., KROEZE, J., NIESSEN, R., ROOSMALEN-VOS, S. V., SPREEUWENBERG, K., KUIPER, C. M., BEEK-VERHOEVEN, N. V. D., KOK, J. J., KNEGTEL, R. M. A., VERMEULEN, A. N.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; amino acid sequences; Amino acids; Animals; antigens; Antigens, Protozoan - genetics; Antigens, Protozoan - immunology; Antigens, Protozoan - isolation & purification; Apicomplexa; Base Sequence; Biological and medical sciences; Blotting, Western - veterinary; Chickens; Cloning; coccidiosis; Coccidiosis - immunology; Coccidiosis - parasitology; Coccidiosis - veterinary; complementary DNA; Dehydrogenase; developmental stages; Eimeria; Eimeria acervulina; Eimeria tenella - enzymology; Eimeria tenella - genetics; Eimeria tenella - immunology; Fundamental and applied biological sciences. Psychology; gene expression; General aspects; General aspects and techniques. Study of several systematic groups. Models; Immunohistochemistry - veterinary; Invertebrates; Isoenzymes; Kinases; L-Lactate Dehydrogenase - chemistry; L-Lactate Dehydrogenase - genetics; L-Lactate Dehydrogenase - immunology; lactate dehydrogenase; Models, Molecular; molecular models; Molecular Sequence Data; nucleotide sequences; Oocysts; Parasites; Plasmodium; Poultry Diseases - parasitology; Protein Conformation; protein synthesis; Proteins; Protozoan Vaccines - chemistry; Protozoan Vaccines - genetics; Protozoan Vaccines - immunology; Reverse Transcriptase Polymerase Chain Reaction - veterinary; RNA, Protozoan - chemistry; RNA, Protozoan - genetics; schizont antigens; Sequence Alignment; Sequence Analysis, DNA; sequence homology; Structure-Activity Relationship; vaccine; vaccine development
• ISSN: 0031-1820; 1469-8161
• DOI: 10.1017/S0031182004005104

An Eimeria acervulina protein fraction was identified which conferred partial protection against an E. acervulina challenge infection. From this fraction a 37 kDa protein was purified and its corresponding cDNA was cloned and shown to encode a lactate dehydrogenase (LDH). Full length cDNAs encoding LDH from two related species, E. tenella and E. maxima, were also cloned. The homology between the primary amino acid sequences of these three Eimeria LDH enzymes was rather low (66–80%), demonstrating an evolutionary divergence. The Plasmodium LDH crystal structure was used to generate a 3D-model structure of E. tenella LDH, which demonstrated that the many variations in the primary amino acid sequences (P. falciparum LDH and E. tenella LDH show only 47% identity) had not resulted in altered 3D-structures. Only a single LDH gene was identified in Eimeria, which was active as a homotetramer. The protein was present at similar levels throughout different parasitic stages (oocysts, sporozoites, schizonts and merozoites), but its corresponding RNA was only observed in the schizont stage, suggesting that its synthesis is restricted to the intracellular stage.