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Structure-Function Implications of the Ability of Monoclonal Antibodies Against alpha-Galactosylceramide-CD1d Complex to Recognize beta-Mannosylceramide Presentation by CD1d

Artikel i vetenskaplig tidskrift
Författare K. Clark
J. Yau
A. Bloom
J. Wang
D. J. Venzon
M. Suzuki
L. Pasquet
B. J. Compton
Susanna Cardell
S. A. Porcelli
G. F. Painter
D. M. Zajonc
J. A. Berzofsky
M. Terabe
Publicerad i Frontiers in Immunology
Volym 10
ISSN 1664-3224
Publiceringsår 2019
Publicerad vid Institutionen för biomedicin, avdelningen för mikrobiologi och immunologi
Språk en
Länkar dx.doi.org/10.3389/fimmu.2019.02355
Ämnesord 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
Ämneskategorier Immunologi inom det medicinska området

Sammanfattning

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.

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Denna text är utskriven från följande webbsida:
http://www.gu.se/forskning/publikation/?publicationId=286226
Utskriftsdatum: 2020-02-21