Allergen Entrapped in Liposomes Reduce Allergenicity and Induce Immunogenicity on Repeated Injections in Mice

Arora, Naveen; Gangal, S. V.

doi:10.1159/000235084

Cited by 13 publications

(3 citation statements)

References 19 publications

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“…In an attempt to increase the safety and effectiveness of desensitization treatments, new forms of presentation of allergens have been sought. The two major approaches to producing greater tolerance in patients are to reduce the frequency of allergen injection by slow release of the allergen and to reduce the allergenicity of the proteins while retaining their immunogenicity (Arora and Gangal., 1990).…”

Section: Introductionmentioning

confidence: 99%

“…Suppression of IgE formation and an increase in IgG titer were verified for mite allergens entrapped in liposomes (Stewart et al, 1988). A more complete set of data on IgE and IgG after repeated injections in mice of allergenic proteins from Artemisia scoparia pollen entrapped in multilamellar liposomes were reported by Arora and Gangal (1990).…”

Section: Introductionmentioning

confidence: 99%

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Preparation and characterization of liposomes entrapping allergenic proteins

Cabral

Zollner

Santana

2004

Braz. J. Chem. Eng.

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-This work presents results of the preparation and characterization of small unilamellar liposomes for entrapping allergenic proteins extracted from the biomass of Dreschlera (Helminthosporium) monoceras cultivated by solid fermentation. Protein was entrapped by the dehydration-rehydration method, using lyophilization of preformed liposomes in order to prevent their degradation The reconstitution of lyophilized liposomes by hydration, their capacity for entrapping allergenic proteins and their stability in plasma were analyzed. Liposomes were reconstituted in size by including trehalose sugar in the formulation. The protection of the liposomal membrane by trehalose was characterized by differential scanning calorimetry and X-ray diffraction. The reconstituted membrane had an osmotic behavior similar to that of nondehydrated ones. Allergenic proteins ranging in molecular weight from 14 to 170 kDa were entrapped in the lipid matrix with an efficiency of approximately 80%. These results are promising for producing liposomes by entrapping allergenic proteins from mold extracts, which can be useful for allergy therapy.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Preparation and characterization of liposomes entrapping allergenic proteins

Cabral

Zollner

Santana

2004

Braz. J. Chem. Eng.

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“…Several investigations with liposome-associated allergens have already yielded promising results (34). Arora & Gangal (4,5) and Ramirez et al (26) studied the tissue distribution of liposome-associated allergens and showed that sustained release from the injection site occurred, particularly xvith MLV. In 1984, Wagner et al (33) shoxved that the incorporation of allergens into liposomes reduced generalized anaphylactic reactions in sensitized animals but conserved antigenicity and increased the production of protective antibodies.…”

mentioning

confidence: 99%

Optimization and characterization of freeze‐dried multilamellar liposomes incorporating different standardized allergen extracts

Genin¹,

Barratt²,

Thao³

et al. 1994

Allergy

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Desensitization therapy for type I allergy is now current practice. Liposomes have been proposed as a support for allergens to improve safety and effectiveness. The aim of this work was to optimize liposomal formulations of three different standardized allergen extracts and to test their allergenicity in vitro and in a preclinical trial. Allergen extracts (Dactylis glomerata, Dermatophagoides pteronyssinus, and cat hair and dander) were associated with multilamellar liposomes of varying compositions at different pH. Liposome-bound allergens were quantified by RAST inhibition after ultracentrifugation, and analyzed qualitatively by SDS-PAGE followed by immunoblotting. Their allergenicity was assessed by basophil degranulation in vitro, as compared with the allergenicity of an aqueous extract, and by skin tests in allergic subjects. The best association, about 50% of the added allergen, was obtained with negatively charged liposomes, when the pH of the allergen solution was adjusted so as to impart a net positive charge to the proteins. One-third of the liposome-associated allergens was located on the surface of the liposomes and was free to interact with antibody, as shown by RAST inhibition assays and the basophil degranulation test; the remaining two-thirds was encapsulated within the liposomes. All the major immunoreactive proteins in the extract were included. These liposomes could be readily freeze-dried and reconstituted without changing their properties. This study reveals the allergenic characteristics of liposomes and suggests their potential use in the treatment of allergic patients.

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