Nomenclature and listing of celiac disease relevant gluten T-cell epitopes restricted by HLA-DQ molecules

Sollid, Ludvig M.; Qiao, Shuo‐Wang; Anderson, Robert P.; Gianfrani, Carmen; Koning, Frits

doi:10.1007/s00251-012-0599-z

Cited by 402 publications

(422 citation statements)

References 46 publications

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“…Identification is further complicated in multiple sclerosis (MS), for example, by the fact that the appropriate target antigen may change over time due to epitope spreading. Nevertheless, in some disorders, including celiac disease, MS, and type 1 diabetes, numerous antigens have been identified [80,[82][83][84]. Another potential strategy, which both harnesses the natural mechanisms that may have initiated autoimmunity and obviates the need for knowing the precise epitopes, may be the use of full-length proteins.…”

Section: Np Development For Tolerancementioning

confidence: 99%

Harnessing Nanoparticles for Immune Modulation

Getts¹,

Shea²,

Miller³

et al. 2016

Trends in Immunology

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Recent approaches using nanoparticles engineered for immune regulation have yielded promising results in preclinical models of disease. The number of nanoparticle therapies is growing, fueled by innovations in nanotechnology and advances in understanding of the underlying pathogenesis of immune-mediated diseases. In particular, recent mechanistic insight into the ways in which nanoparticles interact with the mononuclear phagocyte system and impact its function during homeostasis and inflammation have highlighted the potential of nanoparticle-based therapies for controlling severe inflammation while concurrently restoring peripheral immune tolerance in autoimmune disease. Here we review recent advances in nanoparticle-based approaches aimed at immune-modulation, and discuss these in the context of concepts in polymeric nanoparticle development, including particle modification, delivery and the factors associated with successful clinical deployment.

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Section: Np Development For Tolerancementioning

confidence: 99%

Harnessing Nanoparticles for Immune Modulation

Getts¹,

Shea²,

Miller³

et al. 2016

Trends in Immunology

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“…Additionally, all of the remaining DQ2.2-binding peptides we identified carry serine residues in their sequences, which could potentially be positioned at P3 when bound to the HLA molecule. None of the known DQ2.5 gluten epitopes carries serine at P3 (12). Serine at P3 thus seems to play a crucial role for the differential selection of gluten epitopes by DQ2.5 and DQ2.2.…”

Section: Discussionmentioning

confidence: 96%

“…The gluten T cell epitopes presented by DQ2.5 are fairly well characterized (12). Less is known about the gluten epitopes presented by DQ8 or DQ2.2, and only one DQ2.2 T cell epitope is known (7,12). Typically the gluten peptides that are recognized by T cells of CD patients are posttranslationally modified (13,14).…”

mentioning

confidence: 99%

HLA-DQ Molecules as Affinity Matrix for Identification of Gluten T Cell Epitopes

Dørum

Bodd

Fallang

et al. 2014

The Journal of Immunology

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Even though MHC class II is a dominant susceptibility factor for many diseases, culprit T cell epitopes presented by disease-associated MHC molecules remain largely elusive. T cells of celiac disease lesions recognize cereal gluten epitopes presented by the disease-associated HLA molecules DQ2.5, DQ2.2, or DQ8. Employing celiac disease and complex gluten Ag digests as a model, we tested the feasibility of using DQ2.5 and DQ2.2 as an affinity matrix for identification of disease-relevant T cell epitopes. Known gluten T cell epitope peptides were enriched by DQ2.5, whereas a different set of peptides was enriched by DQ2.2. Of 86 DQ2.2-enriched peptides, four core sequences dominated. One of these core sequences is a previously known epitope and two others are novel epitopes. The study provides insight into the selection of gluten epitopes by DQ2.2. Furthermore, the approach presented is relevant for epitope identification in other MHC class II–associated disorders.

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“…The celiac disease is a model autoimmune disease, in which, contrarily to many other autoimmune diseases, the trigger (gluten), the tight genetic junction (HLA antigens: DQ2 and DQ8), as well as the primary autoimmune reaction [autoantibodies to tissue transglutaminase (tTG)] are known (Fric et al, 2011;Sollid et al, 2012;Tye-Din et al, 2010). This knowledge represents an advantage in the development of new diagnosis and treatment methods, as well as for the development of food analytical techniques that can easily and accurately detect the presence of gluten-related toxic protein fractions, such as gliadins.…”

Section: Gliadins and The Celiac Diseasementioning

confidence: 99%