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Your search keyword '"van Rhijn, I."' showing total 3 results
Start Over Author "van Rhijn, I." Journal international immunology
3 results on '"van Rhijn, I."'

1. The bovine CD1D gene has an unusual gene structure and is expressed but cannot present α-galactosylceramide with a C26 fatty acid

Author

Nguyen, T.K.A., Koets, A.P., Vordermeier, M., Jervis, P.J., Cox, L.R., Graham, S.P., Santema, W.J., Moody, D.B., van Calenbergh, S., Zajonc, D.M., Besra, G.S., van Rhijn, I., Strategic Infection Biology, Dep Infectieziekten Immunologie, and Dep Gezondheidszorg Landbouwhuisdieren

Subjects
Signal peptide, endocrine system, Synthetic antigen, Immunology, CD1, Gene Expression, Galactosylceramides, chemical and pharmacologic phenomena, Ligands, Body Temperature, Cell Line, Mice, Animals, Humans, Immunology and Allergy, Gene, Original Research, chemistry.chemical_classification, Genetics, Base Sequence, biology, Fatty Acids, Fatty acid, hemic and immune systems, General Medicine, Natural killer T cell, Cell biology, carbohydrates (lipids), chemistry, Cell culture, CD1D, biology.protein, Cytokines, Natural Killer T-Cells, Cattle, lipids (amino acids, peptides, and proteins), Antigens, CD1d
Abstract

Although CD1d and NKT cells have been proposed to have highly conserved functions in mammals, data on functions of CD1d and NKT cells in species other than humans and rodents are lacking. Upon stimulation with the CD1d-presented synthetic antigen α-galactosylceramide, human and rodent type I invariant NKT cells release large amounts of cytokines. The two bovine CD1D (boCD1D) genes have structural features that suggest that they cannot be translated into functional proteins expressed on the cell surface. Here we provide evidence that despite an intron–exon structure and signal peptide that are different from all other known CD1 genes, boCD1D can be translated into a protein that is expressed on the cell surface. However, in vivo treatment of cattle (Bos taurus) with 0.1, 1, or 10 µg kg–1 of the most commonly used α-galactosylceramide, which has a C26 fatty acid, did not lead to an increase in body temperature and serum cytokine levels of the animals. This lack of reactivity is not due to a complete inability of boCD1d to present glycosphingolipids because α-galactosylceramide variants with shorter fatty acids could be presented by boCD1d to human NKT cells in vitro. This suggests that the natural ligands of boCD1d are smaller lipids.

Published
2012
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2. Expansion of human gammadelta T cells after in vitro stimulation with Campylobacter jejuni

Author

van Rhijn, I., van den Berg, L.H., Ang, C.W., Admiraal, J., Logtenberg, T., Strategic Infection Biology, Dep Infectieziekten Immunologie, and Neurology

Subjects
T-Lymphocytes, T cell, Immunology, Immunoglobulin Variable Region, Biology, Medical sciences, Peripheral blood mononuclear cell, Campylobacter jejuni, Microbiology, Immune system, Adjuvants, Immunologic, Antigen, medicine, Humans, Immunology and Allergy, Bescherming en bevordering van de menselijke gezondheid, Geneeskunde(GENK), Interleukin-15, Econometric and Statistical Methods: General, Geneeskunde (GENK), T-cell receptor, Receptors, Antigen, T-Cell, gamma-delta, Sequence Analysis, DNA, General Medicine, T lymphocyte, bacterial infections and mycoses, biology.organism_classification, medicine.anatomical_structure, Interleukin-2, Bacterial antigen, Cell Division
Abstract

Campylobacter jejuni is currently the prime cause of food-borne bacterial gastro-enteritis. An important complication of C. jejuni enteritis is Guillain-Barré syndrome (GBS), an immune-mediated disorder of peripheral nerve tissue. Because little is known about T cell reactivity to C. jejuni, we have analyzed the in vitro immune response of normal individuals against five isolates of C. jejuni representing five different serotypes. We found a preferential expansion of peripheral blood gammadelta T cells after exposure to crude sonicates of all five C. jejuni serotypes. Expansion of gammadelta T cells was dependent on the presence of CD4+/alphabeta+ T cells in the cultures or addition of exogenous IL-2 or IL-15. C. jejuni stimulation was mediated via the TCR and appeared to be induced by a non-proteinaceous bacterial antigen, most likely of phosphoantigenic origin.

Published
2003
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3. The bovine CD1D gene has an unusual gene structure and is expressed but cannot present α-galactosylceramide with a C26 fatty acid.

Author

Nguyen TK, Koets AP, Vordermeier M, Jervis PJ, Cox LR, Graham SP, Santema WJ, Moody DB, van Calenbergh S, Zajonc DM, Besra GS, and Van Rhijn I

Subjects
Animals, Antigens, CD1d biosynthesis, Base Sequence, Body Temperature, Cattle, Cell Line, Cytokines blood, Fatty Acids immunology, Gene Expression, Humans, Ligands, Mice, Natural Killer T-Cells immunology, Antigens, CD1d genetics, Antigens, CD1d immunology, Fatty Acids chemistry, Galactosylceramides chemistry, Galactosylceramides immunology
Abstract

Although CD1d and NKT cells have been proposed to have highly conserved functions in mammals, data on functions of CD1d and NKT cells in species other than humans and rodents are lacking. Upon stimulation with the CD1d-presented synthetic antigen α-galactosylceramide, human and rodent type I invariant NKT cells release large amounts of cytokines. The two bovine CD1D (boCD1D) genes have structural features that suggest that they cannot be translated into functional proteins expressed on the cell surface. Here we provide evidence that despite an intron-exon structure and signal peptide that are different from all other known CD1 genes, boCD1D can be translated into a protein that is expressed on the cell surface. However, in vivo treatment of cattle (Bos taurus) with 0.1, 1, or 10 µg kg⁻¹ of the most commonly used α-galactosylceramide, which has a C26 fatty acid, did not lead to an increase in body temperature and serum cytokine levels of the animals. This lack of reactivity is not due to a complete inability of boCD1d to present glycosphingolipids because α-galactosylceramide variants with shorter fatty acids could be presented by boCD1d to human NKT cells in vitro. This suggests that the natural ligands of boCD1d are smaller lipids.

Published
2013
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