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Structure-Function ...
Structure-Function Implications of the Ability of Monoclonal Antibodies Against alpha-Galactosylceramide-CD1d Complex to Recognize beta-Mannosylceramide Presentation by CD1d
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Clark, K. (författare)
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Yau, J. (författare)
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Bloom, A. (författare)
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Wang, J. (författare)
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Venzon, D. J. (författare)
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Suzuki, M. (författare)
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Pasquet, L. (författare)
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Compton, B. J. (författare)
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- Cardell, Susanna, 1959 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för mikrobiologi och immunologi,Institute of Biomedicine, Department of Microbiology and Immunology
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Porcelli, S. A. (författare)
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Painter, G. F. (författare)
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Zajonc, D. M. (författare)
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Berzofsky, J. A. (författare)
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Terabe, M. (författare)
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(creator_code:org_t)
- 2019-10-09
- 2019
- Engelska.
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Ingår i: Frontiers in Immunology. - : Frontiers Media SA. - 1664-3224. ; 10
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https://www.frontier...
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https://gup.ub.gu.se...
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https://doi.org/10.3...
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Abstract
Ämnesord
Stäng
- iNKT cells are CD1d-restricted T cells recognizing lipid antigens. The prototypic iNKT cell-agonist alpha-galactosylceramide (alpha-GalCer) alongside compounds with similar structures induces robust proliferation and cytokine production of iNKT cells and protects against cancer in vivo. Monoclonal antibodies (mAbs) that detect CD1d-alpha-GalCer complexes have provided critical information for understanding of antigen presentation of iNKT cell agonists. Although most iNKT cell agonists with antitumor properties are alpha-linked glycosphingolipids that can be detected by anti-CD1d-alpha-GalCer mAbs, beta-ManCer, a glycolipid with a beta-linkage, induces strong antitumor immunity via mechanisms distinct from those of alpha-GalCer. In this study, we unexpectedly discovered that anti-CD1d-alpha-GalCer mAbs directly recognized beta-ManCer-CD1d complexes and could inhibit beta-ManCer stimulation of iNKT cells. The binding of anti-CD1d-alpha-GalCer mAb with beta-ManCer-CD1d complexes was also confirmed by plasmon resonance and could not be explained by alpha-anomer contamination. The binding of anti-CD1d-alpha-GalCer mAb was also observed with CD1d loaded with another beta-linked glycosylceramide, beta-GalCer (C26:0). Detection with anti-CD1d-alpha-GalCer mAbs indicates that the interface of the beta-ManCer-CD1d complex exposed to the iNKT cell TCR can assume a structure like that of CD1d-alpha-GalCer, despite its disparate carbohydrate structure. These results suggest that certain beta-linked monoglycosylceramides can assume a structural display similar to that of CD1d-alpha-GalCer and that the data based on anti-CD1d-alpha-GalCer binding should be interpreted with caution.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
Nyckelord
- natural killer T cells
- CD1d
- beta-mannosylceramide
- alpha-galactosylceramide
- L363
- t-cell-receptor
- nkt cells
- tumor-immunity
- crystal-structure
- in-vivo
- activation
- stimulation
- antigens
- ligands
- zeta
- Immunology
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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Till lärosätets databas
- Av författaren/redakt...
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Clark, K.
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Yau, J.
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Bloom, A.
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Wang, J.
-
Venzon, D. J.
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Suzuki, M.
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visa fler...
-
Pasquet, L.
-
Compton, B. J.
-
Cardell, Susanna ...
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Porcelli, S. A.
-
Painter, G. F.
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Zajonc, D. M.
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Berzofsky, J. A.
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Terabe, M.
-
visa färre...
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Göteborgs universitet