Manufacture and clinical application of XZY-1 model computer assisted ECG automatic diagnosis system.
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Adolescent↗
Biomedical subjects
J Y Han
Publications and source records attributed to J Y Han.
Molecular and functional characterization of chicken IL-15.
A cDNA encoding chicken interleukin-15 was cloned from a CD4+ T cell hybridoma expression library by screening with a rabbit antibody against a protein fraction of conditioned medium containing T cell growth promoting activity. The chicken IL-15 cDNA contains an open reading frame of 143 amino acids with a single potential N-linked glycosylation site. The predicted m.w. of the encoded protein (16 kDa) matched the size of an immunoreactive band on Western blots of E. coli expressing the recombinant IL-15. Amino acid and nucleotide sequence analyses of chicken IL-15 revealed 31% and 46% identity with bovine IL-15 respectively and lesser homologies to other mammalian IL-15s. Chicken IL-15 contained all 4 highly conserved cysteine residues present in mammalian IL-15 sequences. RT-PCR demonstrated that the chicken IL-15 gene is expressed in many tissues including spleen, intestine, and muscle and in established macrophage, T lymphoma and fibroblast cell lines. Activation of spleen cells with Con A enhanced the expression of IL-15 gene transcripts in a time-dependent manner. CHO-K1 cells transfected with the chicken IL-15 cDNA secreted a biologically active protein supporting the growth of Con A activated spleen lymphocytes. Continuous culture of spleen Con A lymphoblasts with chicken IL-15 over two months resulted in an enriched T lymphocyte population expressing the gammadeltaTCR, CD8alpha, and CD3 cell surface antigens.
Amino Acid Sequence↗
A recombinant Eimeria protein inducing interferon-gamma production: comparison of different gene expression systems and immunization strategies for vaccination against coccidiosis.
A rabbit antiserum against an 18- to 27-kD native protein fraction (F3) from Eimeria acervulina merozoites identified a cDNA (3-1E) containing a 1086-base pair insertion with an open reading frame of 170 amino acids (predicted molecular weight, 18,523). The recombinant 3-1E cDNA expressed in Escherichia coli produced a 60-kD fusion protein and a 23-kD protein after factor Xa treatment of the fusion protein. Both proteins were reactive with the F3 antiserum by western blot analysis. A rabbit antiserum against a synthetic peptide deduced from the amino acid sequence of the 3-1E cDNA reacted with a 27-kD recombinant 3-1E protein expressed in Sf9 insect cells and a 20-kD native protein expressed by E. acervulina sporozoites and Eimeria tenella sporozoites and merozoites. By immunofluorescence staining, a monoclonal antibody produced against the recombinant 3-1E protein reacted with sporozoites and merozoites of E. acervulina, E. tenella, and Eimeria maxima. Spleen lymphocytes from E. acervulina-immune chickens showed antigen-specific proliferation and interferon (IFN)-gamma production upon stimulation with the recombinant 3-1E protein, indicating that the protein activates cell-mediated immunity during coccidiosis. Immunization of chickens with either the E. coli- or Sf9-expressed recombinant 3-1E protein with adjuvant, or direct injection of the 3-1E cDNA, induced protective immunity against live E. acervulina. Simultaneous injection of the recombinant 3-1E protein, or the 3-1E cDNA, with cDNAs encoding chicken IFN-gamma or interleukin (IL)-2/15 further enhanced protective immunity. These results indicate that the recombinant E. acervulina 3-1E cDNA or its polypeptide product may prove useful as vaccines against avian coccidiosis.
Animals↗