Characterization of a <scp>P</scp>ar j 1/<scp>P</scp>ar j 2 mutant hybrid with reduced allergenicity for immunotherapy of <i><scp>P</scp>arietaria</i> allergy

Bonura, Angela; Passantino, Rosa; Costa, Maria Assunta; Montana, Giovanna; Melis, Marcello; Bondı̀, Maria Luisa; Butteroni, Cinzia; Barletta, Bianca; Corinti, Silvia; Felice, Gabriella Di; Colombo, Piergiuseppe

doi:10.1111/j.1365-2222.2011.03938.x

Cited by 23 publications

(15 citation statements)

References 30 publications

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“…However, the Pru p 3 mutant lost the capacity to bind specific IgG antibodies in mice, which could be a problem in the process of a successful immunotherapy [17, 32, 33]. Recently, a hybrid molecule has been characterized as hypoallergenic mutant, and its application in immunotherapy is possible [34]. The two allergenic LTPs from pellitory pollen, Par j 1 and Par j 2, were merged and produced as recombinant proteins.…”

Section: Introductionmentioning

confidence: 99%

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Allergenic Characterization of New Mutant Forms of Pru p 3 as New Immunotherapy Vaccines

Gómez‐Casado

Garrido‐Arandia

Gamboa

et al. 2013

Clinical and Developmental Immunology

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Nowadays, treatment of food allergy only considered the avoidance of the specific food. However, the possibility of cross-reactivity makes this practice not very effective. Immunotherapy may exhibit as a good alternative to food allergy treatment. The use of hypoallergenic molecules with reduced IgE binding capacity but with ability to stimulate the immune system is a promising tool which could be developed for immunotherapy. In this study, three mutants of Pru p 3, the principal allergen of peach, were produced based on the described mimotope and T cell epitopes, by changing the specific residues to alanine, named as Pru p 3.01, Pru p 3.02, and Pru p 3.03. Pru p 3.01 showed very similar allergenic activity as the wild type by in vitro assays. However, Pru p 3.02 and Pru p 3.03 presented reduced IgE binding with respect to the native form, by in vitro, ex vivo, and in vivo assays. In addition, Pru p 3.03 had affected the IgG4 binding capacity and presented a random circular dichroism, which was reflected in the nonrecognition by specific antibodies anti-Pru p 3. Nevertheless, both Pru p 3.02 and Pru p 3.03 maintained the binding to IgG1 and their ability to activate T lymphocytes. Thus, Pru p 3.02 and Pru p 3.03 could be good candidates for potential immunotherapy in peach-allergic patients.

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Section: Introductionmentioning

confidence: 99%

“…The two allergenic LTPs from pellitory pollen, Par j 1 and Par j 2, were merged and produced as recombinant proteins. The hybrid showed a decrease in its allergenic capacity [34]. …”

Section: Introductionmentioning

confidence: 99%

Allergenic Characterization of New Mutant Forms of Pru p 3 as New Immunotherapy Vaccines

Gómez‐Casado

Garrido‐Arandia

Gamboa

et al. 2013

Clinical and Developmental Immunology

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“…This seems to be particularly important for fragment C, which displays a high prevalence of reactivity in our population (about 80% of the patients). It is important to notice that fragments A and C express non-overlapping regions and contain 3 out of 4 of the highly protruding surface exposed loops (Bonura et al, 2012;Colombo et al, 1998) (loops 1 to 3) identified by the 3D modelling, revealing that both fragments contain immunodominant IgE epitopes.…”

Section: Discussionmentioning

confidence: 97%

Multiple IgE recognition on the major allergen of the Parietaria pollen Par j 2

Longo

Costa

Cibella

et al. 2015

Molecular Immunology

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“…[2][3][4]. Such drugs which lose their ability to interact with IgE antibodies are considerably safer and can be used at doses several times higher than doses of the standard allergen extracts.…”

Section: Introductionmentioning

confidence: 99%

Capsulation of house-dust-mite allergens into nanoparticles developed from chitosan and alginate

et al. 2015

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Allergen preparations intended for the specific therapy of IgE mediated allergy must not induce side effects due to IgE binding. To prevent IgE binding, recombinant Der f 1 and Der f 2, major allergens from house dust mites (HDMs) Dermatophagoides farinae, are capsulated into nanoparticles developed from biodegradable polymers. Nanoparticles 80 nm in diameter and with zeta potential +8 mV are generated from amphiphilic chitosan derivative N-lauryl-N'-succinoylchitosan (LSC). Der f 1 and Der f 2 proteins are introduced during nanoparticle formation. To cover allergens additionally, nanoparticles are coated by an alginate shell. As a result of polyelectrolyte interaction between positively charged LSC and negatively charged alginic acid, constructions of the "core-shell" type are formed which are 90-140 nm in diameter and zeta potential is -13 to -20 mV. We demonstrate that the capsulation of allergens into LSC nanoparticles significantly decreases IgE reactivity while core-shell construction masks the allergens completely, as was shown using IgE positive sera from patients allergic to HDMs. We conclude that constructions of a core-shell type with allergens incorporated in the core particles could increase the safety of preparations for the specific immunotherapy of allergies.

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Characterization of a Par j 1/Par j 2 mutant hybrid with reduced allergenicity for immunotherapy of Parietaria allergy

Cited by 23 publications

References 30 publications

Allergenic Characterization of New Mutant Forms of Pru p 3 as New Immunotherapy Vaccines

Allergenic Characterization of New Mutant Forms of Pru p 3 as New Immunotherapy Vaccines

Multiple IgE recognition on the major allergen of the Parietaria pollen Par j 2

Capsulation of house-dust-mite allergens into nanoparticles developed from chitosan and alginate

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