Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis
Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids wit...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Aspeslagh, Sandrine [verfasserIn] Li, Yali [verfasserIn] Yu, Esther Dawen [verfasserIn] Pauwels, Nora [verfasserIn] Trappeniers, Matthias [verfasserIn] Girardi, Enrico [verfasserIn] Decruy, Tine [verfasserIn] Van Beneden, Katrien [verfasserIn] Venken, Koen [verfasserIn] Drennan, Michael [verfasserIn] Leybaert, Luc [verfasserIn] Wang, Jing [verfasserIn] Franck, Richard W [verfasserIn] Van Calenbergh, Serge [verfasserIn] Zajonc, Dirk M [verfasserIn] Elewaut, Dirk [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2011 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 2011 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 30(2011), 11 vom: 06. Mai, Seite 2294-2305 |
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| Übergeordnetes Werk: |
volume:30 ; year:2011 ; number:11 ; day:06 ; month:05 ; pages:2294-2305 |
| Links: |
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| DOI / URN: |
10.1038/emboj.2011.145 |
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| Katalog-ID: |
SPR058011196 |
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| 245 | 1 | 0 | |a Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis |
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| 520 | |a Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. | ||
| 520 | |a Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. | ||
| 650 | 4 | |a CD1d |7 (dpeaa)DE-He213 | |
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| 650 | 4 | |a iNKT cells |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Li, Yali |e verfasserin |4 aut | |
| 700 | 1 | |a Yu, Esther Dawen |e verfasserin |4 aut | |
| 700 | 1 | |a Pauwels, Nora |e verfasserin |4 aut | |
| 700 | 1 | |a Trappeniers, Matthias |e verfasserin |4 aut | |
| 700 | 1 | |a Girardi, Enrico |e verfasserin |4 aut | |
| 700 | 1 | |a Decruy, Tine |e verfasserin |4 aut | |
| 700 | 1 | |a Van Beneden, Katrien |e verfasserin |4 aut | |
| 700 | 1 | |a Venken, Koen |e verfasserin |4 aut | |
| 700 | 1 | |a Drennan, Michael |e verfasserin |4 aut | |
| 700 | 1 | |a Leybaert, Luc |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Jing |e verfasserin |4 aut | |
| 700 | 1 | |a Franck, Richard W |e verfasserin |4 aut | |
| 700 | 1 | |a Van Calenbergh, Serge |e verfasserin |4 aut | |
| 700 | 1 | |a Zajonc, Dirk M |e verfasserin |4 aut | |
| 700 | 1 | |a Elewaut, Dirk |e verfasserin |4 aut | |
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10.1038/emboj.2011.145 doi (DE-627)SPR058011196 (SPR)emboj.2011.145-e DE-627 ger DE-627 rakwb eng Aspeslagh, Sandrine verfasserin aut Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. CD1d (dpeaa)DE-He213 glycolipids (dpeaa)DE-He213 iNKT cells (dpeaa)DE-He213 Li, Yali verfasserin aut Yu, Esther Dawen verfasserin aut Pauwels, Nora verfasserin aut Trappeniers, Matthias verfasserin aut Girardi, Enrico verfasserin aut Decruy, Tine verfasserin aut Van Beneden, Katrien verfasserin aut Venken, Koen verfasserin aut Drennan, Michael verfasserin aut Leybaert, Luc verfasserin aut Wang, Jing verfasserin aut Franck, Richard W verfasserin aut Van Calenbergh, Serge verfasserin aut Zajonc, Dirk M verfasserin aut Elewaut, Dirk verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 11 vom: 06. Mai, Seite 2294-2305 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:11 day:06 month:05 pages:2294-2305 https://dx.doi.org/10.1038/emboj.2011.145 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 11 06 05 2294-2305 |
| spelling |
10.1038/emboj.2011.145 doi (DE-627)SPR058011196 (SPR)emboj.2011.145-e DE-627 ger DE-627 rakwb eng Aspeslagh, Sandrine verfasserin aut Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. CD1d (dpeaa)DE-He213 glycolipids (dpeaa)DE-He213 iNKT cells (dpeaa)DE-He213 Li, Yali verfasserin aut Yu, Esther Dawen verfasserin aut Pauwels, Nora verfasserin aut Trappeniers, Matthias verfasserin aut Girardi, Enrico verfasserin aut Decruy, Tine verfasserin aut Van Beneden, Katrien verfasserin aut Venken, Koen verfasserin aut Drennan, Michael verfasserin aut Leybaert, Luc verfasserin aut Wang, Jing verfasserin aut Franck, Richard W verfasserin aut Van Calenbergh, Serge verfasserin aut Zajonc, Dirk M verfasserin aut Elewaut, Dirk verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 11 vom: 06. Mai, Seite 2294-2305 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:11 day:06 month:05 pages:2294-2305 https://dx.doi.org/10.1038/emboj.2011.145 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 11 06 05 2294-2305 |
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10.1038/emboj.2011.145 doi (DE-627)SPR058011196 (SPR)emboj.2011.145-e DE-627 ger DE-627 rakwb eng Aspeslagh, Sandrine verfasserin aut Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. CD1d (dpeaa)DE-He213 glycolipids (dpeaa)DE-He213 iNKT cells (dpeaa)DE-He213 Li, Yali verfasserin aut Yu, Esther Dawen verfasserin aut Pauwels, Nora verfasserin aut Trappeniers, Matthias verfasserin aut Girardi, Enrico verfasserin aut Decruy, Tine verfasserin aut Van Beneden, Katrien verfasserin aut Venken, Koen verfasserin aut Drennan, Michael verfasserin aut Leybaert, Luc verfasserin aut Wang, Jing verfasserin aut Franck, Richard W verfasserin aut Van Calenbergh, Serge verfasserin aut Zajonc, Dirk M verfasserin aut Elewaut, Dirk verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 11 vom: 06. Mai, Seite 2294-2305 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:11 day:06 month:05 pages:2294-2305 https://dx.doi.org/10.1038/emboj.2011.145 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 11 06 05 2294-2305 |
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10.1038/emboj.2011.145 doi (DE-627)SPR058011196 (SPR)emboj.2011.145-e DE-627 ger DE-627 rakwb eng Aspeslagh, Sandrine verfasserin aut Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. CD1d (dpeaa)DE-He213 glycolipids (dpeaa)DE-He213 iNKT cells (dpeaa)DE-He213 Li, Yali verfasserin aut Yu, Esther Dawen verfasserin aut Pauwels, Nora verfasserin aut Trappeniers, Matthias verfasserin aut Girardi, Enrico verfasserin aut Decruy, Tine verfasserin aut Van Beneden, Katrien verfasserin aut Venken, Koen verfasserin aut Drennan, Michael verfasserin aut Leybaert, Luc verfasserin aut Wang, Jing verfasserin aut Franck, Richard W verfasserin aut Van Calenbergh, Serge verfasserin aut Zajonc, Dirk M verfasserin aut Elewaut, Dirk verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 11 vom: 06. Mai, Seite 2294-2305 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:11 day:06 month:05 pages:2294-2305 https://dx.doi.org/10.1038/emboj.2011.145 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 11 06 05 2294-2305 |
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10.1038/emboj.2011.145 doi (DE-627)SPR058011196 (SPR)emboj.2011.145-e DE-627 ger DE-627 rakwb eng Aspeslagh, Sandrine verfasserin aut Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2011 Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. CD1d (dpeaa)DE-He213 glycolipids (dpeaa)DE-He213 iNKT cells (dpeaa)DE-He213 Li, Yali verfasserin aut Yu, Esther Dawen verfasserin aut Pauwels, Nora verfasserin aut Trappeniers, Matthias verfasserin aut Girardi, Enrico verfasserin aut Decruy, Tine verfasserin aut Van Beneden, Katrien verfasserin aut Venken, Koen verfasserin aut Drennan, Michael verfasserin aut Leybaert, Luc verfasserin aut Wang, Jing verfasserin aut Franck, Richard W verfasserin aut Van Calenbergh, Serge verfasserin aut Zajonc, Dirk M verfasserin aut Elewaut, Dirk verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 30(2011), 11 vom: 06. Mai, Seite 2294-2305 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:30 year:2011 number:11 day:06 month:05 pages:2294-2305 https://dx.doi.org/10.1038/emboj.2011.145 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 30 2011 11 06 05 2294-2305 |
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Enthalten in The EMBO Journal 30(2011), 11 vom: 06. Mai, Seite 2294-2305 volume:30 year:2011 number:11 day:06 month:05 pages:2294-2305 |
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Aspeslagh, Sandrine @@aut@@ Li, Yali @@aut@@ Yu, Esther Dawen @@aut@@ Pauwels, Nora @@aut@@ Trappeniers, Matthias @@aut@@ Girardi, Enrico @@aut@@ Decruy, Tine @@aut@@ Van Beneden, Katrien @@aut@@ Venken, Koen @@aut@@ Drennan, Michael @@aut@@ Leybaert, Luc @@aut@@ Wang, Jing @@aut@@ Franck, Richard W @@aut@@ Van Calenbergh, Serge @@aut@@ Zajonc, Dirk M @@aut@@ Elewaut, Dirk @@aut@@ |
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Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. 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Aspeslagh, Sandrine |
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Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis CD1d (dpeaa)DE-He213 glycolipids (dpeaa)DE-He213 iNKT cells (dpeaa)DE-He213 |
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Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis |
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Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis |
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Aspeslagh, Sandrine Li, Yali Yu, Esther Dawen Pauwels, Nora Trappeniers, Matthias Girardi, Enrico Decruy, Tine Van Beneden, Katrien Venken, Koen Drennan, Michael Leybaert, Luc Wang, Jing Franck, Richard W Van Calenbergh, Serge Zajonc, Dirk M Elewaut, Dirk |
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Elektronische Aufsätze |
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galactose‐modified inkt cell agonists stabilized by an induced fit of cd1d prevent tumour metastasis |
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Galactose‐modified iNKT cell agonists stabilized by an induced fit of CD1d prevent tumour metastasis |
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Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. © European Molecular Biology Organization 2011 |
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Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. © European Molecular Biology Organization 2011 |
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Abstract Invariant natural killer T (iNKT) cells are known to have marked immunomodulatory capacity due to their ability to produce copious amounts of effector cytokines. Here, we report the structure and function of a novel class of aromatic α‐galactosylceramide structurally related glycolipids with marked Th1 bias in both mice and men, leading to superior tumour protection in vivo. The strength of the Th1 response correlates well with enhanced lipid binding to CD1d as a result of an induced fit mechanism that binds the aromatic substitution as a third anchor, in addition to the two lipid chains. This induced fit is in contrast to another Th1‐biasing glycolipid, α‐C‐GalCer, whose CD1d binding follows a conventional key‐lock principle. These findings highlight the previously unexploited flexibility of CD1d in accommodating galactose‐modified glycolipids and broaden the range of glycolipids that can stimulate iNKT cells. We speculate that glycolipids can be designed that induce a similar fit, thereby leading to superior and more sustained iNKT cell responses in vivo. Abstract Invariant natural killer T (iNKT) cells are activated by lipid derivatives presented by the non‐classical MHC I molecule CD1d. Galactose‐modified glycolipids enhance the affinity of glycolipids for CD1d, leading to sustained iNKT cell responses and tumour protection in vivo. © European Molecular Biology Organization 2011 |
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|
| score |
7.401019 |