Mapping of conformational IgE epitopes on Phl p 5a by using mimotopes from a phage display library

Hantusch, Brigitte; Krieger, Sigurd; Untersmayr, Eva; Schöll, Isabella; Knittelfelder, Regina; Flicker, Sabine; Spitzauer, Susanne; Valenta, Rudolf; Boltz‐Nitulescu, George; Scheiner, Otto; Jensen‐Jarolim, Erika

doi:10.1016/j.jaci.2004.06.048

Cited by 53 publications

(45 citation statements)

References 39 publications

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“…In these studies, the potential of protein-based mimotopes for allergy immunotherapy was demonstrated by the induction of anti-mimotope antibodies in BALB/c mice which were co-reactive with Phl p 5 [3].…”

Section: Discussionmentioning

confidence: 99%

“…In a previous study, peptide mimotope F1 was identified as a specific epitope-mimic (mimotope) of grass pollen major allergen Phl p 5 by screening a phage display library with Phl p 5-specific IgE [3]. The peptide library consisted of decameric peptides presented on minor phage coat protein pIII of filamentous phage M13.…”

Section: Construction Of the Dna Immunization Vectors Pcmv-f1 And Pcmmentioning

confidence: 99%

“…The selected mimics resemble IgE binding epitopes of the allergen surface by virtue of their physico-chemical properties [1]. In peptide form, such epitope-mimics (mimotopes) have repeatedly been shown to induce epitope-specific, allergen-specific immune responses [2][3][4][5][6]. Due to the fact that mimotopes do not contain allergen-specific T-cell epitopes, the immune responses towards mimotopes depend on the recruitment of bystander Th-cells.…”

Section: Introductionmentioning

confidence: 99%

“…The mimotope-induced IgG antibodies are then directed not only against the mimotopes, but co-recognize the 3-dimensional allergen epitope via molecular mimicry. Therefore, they are able to prevent the high-affinity interaction between allergen and specific IgE antibodies [3,8] and thus can be called blocking antibodies [9,10]. In several studies we and others have already characterized peptides and anti-idiotypic Fab fragments being mimotopes of different allergens and antigens [2,6,[11][12][13].…”

Section: Introductionmentioning

confidence: 99%

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A mimotope gene encoding the major IgE epitope of allergen Phl p 5 for epitope-specific immunization

et al. 2009

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A gene vaccine based on a mammalian expression vector containing the sequence of a peptide mimotope of Phl p 5 was constructed. To test whether mimotope gene vaccines can induce allergen-specific antibody responses via molecular mimicry, BALB/c mice were immunized using the mimotope construct with or without a tetanus toxin T-helper epitope. Moreover, intradermal injection was compared to epidermal application via gene gun immunization.Immunization with both mimotope gene constructs elicited allergen-specific antibody responses. As expected, gene gun bombardment induced a Th2-biased immune response, typically associated with IgG1 and IgE antibody production. In contrast, intradermal injection of the vaccine triggered IgG2a antibody expression without any detectable IgE levels, thus biasing the immune response towards Th1. In an RBL assay, mimotope-specific IgG antibodies were able to prevent crosslinking of allergen-specific IgE by Phl p 5. A construct coding for the complete Phl p 5 induced Tcell activation, IFN-γ and IL-4 production. In contrast, the mimotope-DNA construct being devoid of allergen-specific T-cell epitopes had no capacity to activate allergen-specific T cells.Taken together, our data show that it is feasible to induce blocking IgG antibodies with a mimotope-DNA construct when applied intradermally. Thus the mimotope-DNA strategy has two advantages: (1) the avoidance of IgE induction and (2) the avoidance of triggering allergenspecific T-lymphocytes. We therefore suggest that mimotope gene vaccines are potential candidates for epitope-specific immunotherapy of type I allergy.

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Section: Discussionmentioning

confidence: 99%

Section: Construction Of the Dna Immunization Vectors Pcmv-f1 And Pcmmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A mimotope gene encoding the major IgE epitope of allergen Phl p 5 for epitope-specific immunization

et al. 2009

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“…In this group, researchers most often published data from IAsys (Affinity Sensors ), Spreeta and TISPR-1 (Texas Instruments [978][979][980][981][982][983][984][985][986][987][988][989][990][991][992] , small molecules , and cells, phage and virus particles [866][867][868][869][870][871][872][873][874][875][876][877][878][879][880][881][882][883][884][885]. In the applied sciences, biosensors increasingly contribute in clinical [886][887][888][889][890][891][892][893][894][895][896][897][898][899]…”

Section: Instrumentsmentioning

confidence: 99%

Survey of the year 2004 commercial optical biosensor literature

Rich

Myszka

2005

J of Molecular Recognition

115

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The year 2004 represents a milestone for the biosensor research community: in this year, over 1000 articles were published describing experiments performed using commercially available systems. The 1038 papers we found represent a $ 10% increase over the past year and demonstrate that the implementation of biosensors continues to expand at a healthy pace. We evaluated the data presented in each paper and compiled a 'top 10' list. These 10 articles, which we recommend every biosensor user reads, describe wellperformed kinetic, equilibrium and qualitative/screening studies, provide comparisons between binding parameters obtained from different biosensor users, as well as from biosensor-and solution-based interaction analyses, and summarize the cutting-edge applications of the technology. We also re-iterate some of the experimental pitfalls that lead to sub-optimal data and over-interpreted results. We are hopeful that the biosensor community, by applying the hints we outline, will obtain data on a par with that presented in the 10 spotlighted articles. This will ensure that the scientific community at large can be confident in the data we report from optical biosensors.

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Fine mapping of a monoclonal antibody to the N‐Methyl D‐aspartate receptor reveals a short linear epitope

et al. 2012

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Anti-N-Methyl D-aspartate receptor encephalitis is an autoimmune disease in which autoantibodies are produced against extracellular regions of the N-Methyl D-aspartate receptor (NMDAR). In this study, we used resin-bound peptides equipped with a base labile linker to map the epitope of a monoclonal NMDAR antibody against the NMDAR NR1 subunit. The antigenicity of the synthesized resin-bound peptides was determined by enzyme-linked immunosorbent assay. Distinct reactivity was found to two extracellular overlapping peptides (amino acids, 658-687). Using N- and C-terminally truncated resin-bound peptides, the minimum functional epitope was identified as the NPSDK sequence. The peptide sequence RNPSDK (amino acids, 673-678) was identified as the complete epitope, which was found to be located in the extracellular S2 domain of the NR1 subunit. Especially, the N-terminal arginine residue was found to be essential for reactivity, whereas the remaining amino acids could be replaced with amino acids of similar side-chain functionality, indicating the importance of backbone interaction in antibody reactivity.

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Mapping of conformational IgE epitopes on Phl p 5a by using mimotopes from a phage display library

Cited by 53 publications

References 39 publications

A mimotope gene encoding the major IgE epitope of allergen Phl p 5 for epitope-specific immunization

A mimotope gene encoding the major IgE epitope of allergen Phl p 5 for epitope-specific immunization

Survey of the year 2004 commercial optical biosensor literature

Fine mapping of a monoclonal antibody to the N‐Methyl D‐aspartate receptor reveals a short linear epitope

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