Recombinant Amb a 1 expression

The number of identified pollen allergens, especially homologues belonging to the group of pectate lyases, is constantly rising. The main allergenic protein of common ragweed (Ambrosia artemisiifolia) Amb a 1 resembles the most prominent specimen. The major allergens from pollen of cedar, juniper and cypress species Jun a 1 (Juniperus ashei), Cry j 1 (Cryptomeria japonica), Cup a 1 (Cupressus arizonica) and Cha o 1 (Chamaecyparis obtuse) as well as Art v 6 from Mugwort (Artemisia vulgaris) also belong to the family of pectate lyases. Pectate lyases themselves resemble a large group of enzymes not only expressed in ripening fruits and in plant pathogenic bacteria, but also in pollen. These enzymes are able to digest the pectin or pectate envelope of plant cells. Although enzymatic activity is not shown for all above mentioned allergens, the high homology on aminoacid level and the cross-reactivity of patient s sera especially within the conifers unify this group. In the U.S. about 50% of all allergic individuals (including patients with food, dust, mite and other allergies) suffer from ragweed pollinosis (hay fever). This shows the magnitude of the ragweed problem. Since ragweed already started invading parts of France, Hungary, Germany, Finland and Austria, this very potent, allergy provoking plant will soon cause big problems in Europe, too. Accurate standardization of natural pollen extracts is a difficult task. Thus there is a need for reliable and effective diagnostic and therapeutic tools for allergy treatment. Therefore the production of soluble recombinant allergens of the pectate lyase group is an important task. For this purpose we were evaluating the plant-based expression systems for Amb a1