– AllerR induces formation of antibodies recognizing natural ragweed allergens –
Anergis, a company developing breakthrough allergy vaccines for fast and safe allergen-specific immunotherapy, reported today that it will present preclinical data for its ragweed allergy vaccine at the 2013 Annual Meeting of the American Academy of Allergy, Asthma & Immunology (AAAAI) in San Antonio, TX.*
The results demonstrate the hypoallergenicity of AllerR and the successful recognition of the natural ragweed allergen Amb a 1 by the mouse immune system after immunization with AllerR.
The poster no. 136 will be presented on Saturday, February 23, 2013, at 9:45am CST in session no. 2210 “Immunotherapy I” at the Henry B. Gonzalez Convention Center, Street Level, Exhibit Hall C. The abstract of the poster titled “Non-Detectable IgE Binding of an Amb a 1 Derived, Contiguous Overlapping Peptide Based, SIT Product Candidate Against Ragweed Allergy” is available at:
AllerR is a mix of seven Contiguous Overlapping Peptides (COPs) derived from the COP platform of Anergis. In the experiments, AllerR showed no detectable IgE binding in competition ELISA tests using sera from allergic patients and did not induce degranulation of humanized basophil cells, a standard test used to test the ability of a protein or peptide to elicit an allergic reaction in humans. In addition, mice sensitized to the natural allergen Amb a 1 showed no reactivity to AllerR, whereas the administration of Amb a 1 in these animals lead to anaphylactic responses. The immunogenicity of AllerR was also tested in naïve mice and showed that each COP composing AllerR elicited an antibody response and that these antibodies specifically recognized the natural Amb a 1 allergen.
In the U.S., ragweed pollen allergy is the major cause of hay fever: 75% of all patients suffering from pollen allergies carry a ragweed pollen allergy. It affects about 20% of the U.S. population and is also on the rise in Europe due to the spread of ragweed (Ambrosia genus) plants accidentally introduced to Europe. The major allergenic protein has been identified as Amb a 1, a 38 kDa non-glycosylated protein composed of two subunits.
* The poster entitled “Non-Detectable IgE Binding of an Amb a 1 Derived, Contiguous Overlapping Peptide Based, SIT Product Candidate Against Ragweed Allergy” is also being published in The Journal of Allergy and Clinical Immunology – February 2013 (Vol. 131, Issue 2, Supplement, Page AB37, DOI: 10.1016/j.jaci.2012.12.815)