Abstract: The present invention provides herbal compositions that can prevent or reduce the severity, intensity, or duration of allergic and/or asthmatic symptoms and/or can prevent or delay the development of an allergic or asthmatic response to an antigen. The compositions may optionally include one or more adjuvants, cytokines, encapsulating materials, or pharmaceutical carriers or excipients, and may be administered prior to, during, or after the development of allergic or asthmatic symptoms in sensitized individuals. Alternatively or additionally, the compositions may be administered prior to sensitization to a particular antigen; preferably substantially concurrently with exposure to the antigen.

Abstract: The present invention provides an animal model for studying allergic reactions to allergens. The animal is sensitized to a selected antigen by administering the antigen itself or a nucleic acid encoding the antigen. Preferred antigens are anaphylactic antigens. The sensitized animal can then be used to screen for compounds which may help to prevent, ameliorate, or cure allergic conditions in humans. A method of sensitizing an animal as well as a method and system for screening chemical compounds is also disclosed.

Abstract: It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity. The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined.

Abstract: Peanuts are a common cause of food hypersensitivity reactions. The sera of 10 patients who had atopic dermatitis and a positive double-blind placebo-controlled food challenge to peanut were used to investigate the major allergens of peanut. Crude Florunner extracts were fractionated by anion-exchange chromatography using a step gradient (limit buffer, 0.05M BisTris/1.5M NaCl). A protein peak (OD 280) which eluted at 10% NaCl and demonstrated intense IgE-binding was further analyzed by two-dimensional SDS-PAGE/immunoblot analysis. The majority of this fraction is a protein which has a molecular weight of 17 kD and a pI of 5.2. Sequencing data from the N-terminus revealed the following initial 9 amino acids: (*)-Q-Q-(*)-E-L-Q-D-L. Based on IgE-binding activity and no known amino acid sequence identity to other allergens, this allergen is designated Ara h II. Ara h II may be used to detect and quantify peanut allergens in foodstuffs.

Abstract: Nanoparticle coacervates of nucleic acids and polycations serve as effective vaccines when administered orally. They can induce immunity to a variety of disease causing agents and raise a protective response to allergens.

Abstract: Formulations and methods have been developed for delivering antigens to individuals in a manner that substantially reduces contact between the antigen and IgE receptors displayed on the surfaces of cells involved in mediating allergic responses, which target delivery of antigen to dendritic and other phagocytic APCs, and which have improved pharmacokinetics. By reducing direct and indirect association of antigens with antigen-specific IgE antibodies, the risk of an allergic reaction, possibly anaphylatic shock, is reduced or eliminated. Particularly preferred antigens are those that may elicit anaphylaxis in individuals, including food antigens, insect venom and rubber-related antigens. In the preferred embodiments, the compositions include one or more antigens in a delivery material such as a polymer, in the form of particles or a gel, or lipid vesicles or liposomes, any of which can be stabilized or targeted to enhance delivery. Preferably, the antigen is surrounded by the encapsulation material.

Abstract: It has been discovered that one can predict the likelihood a child will outgrow an allergy, especially a food allergy, by screening for IgE antibodies immunoreactivities with linear versus conformational epitopes. The child is first screened using standard techniques to determine what antigens the child is allergic to. The immunoglobulins in the sample from the patient are then characterized either using the natural purified antigen, recombinant antigen, reduced and alkylated antigen, proteolytic fragments of the antigen or synthetic peptides of between four and 40 amino acids in length, preferably six to ten amino acids, which can be immobilized for rapid and accurate screening. The antibodies from the patient, typically present in a serum or plasma sample, are reacted with the protein or peptides to determine which peptides are bound by the antibodies. These antibodies are then characterized to determine if the epitopes they bind are linear or conformational.