Major T cell epitope-containing peptides can elicit strong antibody responses

Wu, Bo; Toussaint, G; Elst, Luc Vander; Granier, Claude; Jacquemin, Marc; Saint-Remy, Jean-Marie

doi:10.1002/1521-4141(200001)30:1<291::aid-immu291>3.0.co;2-t

Cited by 21 publications

(27 citation statements)

References 20 publications

(28 reference statements)

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“…We have previously shown that substitution of Ile 28 by Ala or Asn abolishes p21-35-induced T cell proliferation (19), and we now demonstrate that this is accompanied by a significant reduction in IFN-␥ production. The latter was not affected by the Lys 33 Ala substitution, which eliminates the major p21-35 B cell epitope (19). The production of cytokines by polyclonal T cells toward p21-35, however, could have been biased by the use of CFA (28).…”

Section: P21-35 Elicits Th1-like Cytokines In Vitrosupporting

confidence: 69%

“…We have previously shown that BALB/c mice (H-2 d ) produce high titers of specific Abs upon immunization with Der p 2 and that a T cell epitope is located between residues 21 and 35 (19). To determine whether the T cell epitope is dominant, T cells were prepared from LN cells of six BALB/c mice primed by s.c. footpad injection of rDer p 2 and were pooled and restimulated in vitro with a series of 15-mer overlapping peptides spanning the entire Der p 2 sequence.…”

Section: P21-35 Is Recognized In the Context Of Different Mhc Class Imentioning

confidence: 99%

“…6B). In a previous study, Ile 28 had been identified using known algorithms as a putative P4 anchoring residue in H-2 d haplotype (19,30). Because the T cell epitopes defined for H-2 k and H-2 s mice are almost identical (Fig.…”

Section: Ile 28 Is Critical For T Cell Responses In Different Mhc Hapmentioning

confidence: 99%

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TheDermatophagoides pteronyssinusGroup 2 Allergen Contains a Universally Immunogenic T Cell Epitope

Elst

Carlier

et al. 2002

The Journal of Immunology

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The use of T cell epitope-containing peptides for the induction of anergy in allergen sensitization is limited by genetic restriction that could be circumvented by using universally immunogenic epitopes. We attempted to identify such epitopes on Dermatophagoides pteronyssinus group 2 allergen (Der p 2), a major allergen of D. pteronyssinus T cells from BALB/c (H-2d), C57BL/6 (H-2b), C3H (H-2k), and SJL (H-2s) mice that were immunized with rDer p 2, recognized an immunodominant region encompassing residues 21–35. A synthetic 21–35 peptide (p21–35) induced strong dose-dependent in vitro T cell proliferation with cells of the four mouse strains and required processing for MHC class II presentation. Substitution of Ile28 with Ala resulted in reduction of T cell proliferation in each strain. Ile28 could represent an important MHC class II anchoring residue for T cell response to p21–35. An immunodominant T cell epitope of Der p 2 therefore behaves as a universal epitope and could be a suitable candidate for T cell anergy induction.

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Section: P21-35 Elicits Th1-like Cytokines In Vitrosupporting

confidence: 69%

Section: P21-35 Is Recognized In the Context Of Different Mhc Class Imentioning

confidence: 99%

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TheDermatophagoides pteronyssinusGroup 2 Allergen Contains a Universally Immunogenic T Cell Epitope

Elst

Carlier

et al. 2002

The Journal of Immunology

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“…p21-35 has been extensively studied in our laboratory: it contains both a major promiscuous T cell epitope and a dominant B epitope (17), thereby providing a suitable sequence for the study of tolerance induction at B and T cell levels. Injection of p21-35 in conventional adjuvant elicits strong specific Ab responses, while the same peptide under tolerogenic conditions results in prevention and partial suppression of the immune response toward Der p 2 (18). To ensure efficient presentation of the Ag to CD4…”

Section: In Vivo Induction Of Type 1-like Regulatory T Cells Using Gementioning

confidence: 99%

In Vivo Induction of Type 1-Like Regulatory T Cells Using Genetically Modified B Cells Confers Long-Term IL-10-Dependent Antigen-Specific Unresponsiveness

Ahangarani

Janssens

VanderElst

et al. 2009

The Journal of Immunology

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“…One disadvantage of SIT is that the administration of allergenic material may cause severe and lifethreatening anaphylactic side effects (1). This problem can be bypassed by using isoforms of allergens (2), deletion mutants (3), fragments of proteins (4,5), or linear peptides (6) that lack the original IgE-binding epitopes. The use of engineered "hypoallergenic" variants with reduced IgE reactivity is now being explored in several systems (7,8).…”

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confidence: 99%

Construction of Hevein (Hev b 6.02) with Reduced Allergenicity for Immunotherapy of Latex Allergy by Comutation of Six Amino Acid Residues on the Conformational IgE Epitopes

Karisola

Mikkola

Kalkkinen

et al. 2004

The Journal of Immunology

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Recently we have established that IgE Abs bind to conformational epitopes in the N- and C-terminal regions of the major natural rubber latex allergen, hevein (Hev b 6.02). To identify the critical amino acid residues that interact with IgE, the hevein sequence was scanned by using site-specific mutations. Twenty-nine hevein mutants were designed and produced by a baculovirus expression system in insect cells and tested by IgE inhibition-ELISA using sera from 26 latex allergic patients. Six potential IgE-interacting residues of hevein (Arg5, Lys10, Glu29, Tyr30, His35, and Gln38) were identified and characterized further in detail. Based on these six residues, two triple mutants (HΔ3A, HΔ3B) and hevein mutant where all six residues were mutated (HΔ6), were designed, modeled, and produced. Structural and functional properties of these combinatory mutants were compared experimentally and in silico with those of recombinant hevein. The IgE-binding affinity of the mutants decreased by three to five orders of magnitude as compared with that of recombinant hevein. Skin prick test reactivity of the triple mutant HΔ3A was drastically reduced and that of the six-residue mutant HΔ6 was completely abolished in all patients examined in this study. The approach presented in this paper offers tools for identification and modification of amino acid residues on conformational epitopes of allergens that interact with IgE. Hevein with a highly reduced ability to bind IgE should provide a valuable candidate molecule for immunotherapy of latex allergy and is anticipated to have a low risk of systemic side effects.

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Major T cell epitope-containing peptides can elicit strong antibody responses

Cited by 21 publications

References 20 publications

TheDermatophagoides pteronyssinusGroup 2 Allergen Contains a Universally Immunogenic T Cell Epitope

TheDermatophagoides pteronyssinusGroup 2 Allergen Contains a Universally Immunogenic T Cell Epitope

In Vivo Induction of Type 1-Like Regulatory T Cells Using Genetically Modified B Cells Confers Long-Term IL-10-Dependent Antigen-Specific Unresponsiveness

Construction of Hevein (Hev b 6.02) with Reduced Allergenicity for Immunotherapy of Latex Allergy by Comutation of Six Amino Acid Residues on the Conformational IgE Epitopes

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