Recombinant Amb a 1 expression

Georg Schmidt, N. Wopfner, F. Ferreira, Anneli Ritala

Research output: Chapter in Book/Report/Conference proceedingConference abstract in proceedingsScientific

Abstract

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.
Original languageEnglish
Title of host publicationPlants for Human Health in the Post-Genome Era
Subtitle of host publicationPSE Congress
Place of PublicationEspoo
PublisherVTT Technical Research Centre of Finland
Pages125-125
ISBN (Electronic)978-951-38-6322-7
ISBN (Print)978-951-38-6321-0
Publication statusPublished - 2007
EventPSE Congress: Plants for Human Health in the Post-Genome Era - Helsinki, Finland
Duration: 26 Aug 200729 Aug 2007

Publication series

SeriesVTT Symposium
Number249

Conference

ConferencePSE Congress: Plants for Human Health in the Post-Genome Era
CountryFinland
CityHelsinki
Period26/08/0729/08/07

Fingerprint

pectate lyase
allergens
hypersensitivity
pollen
Artemisia vulgaris
hay fever
Cupressus arizonica
Juniperus ashei
Chamaecyparis
Ambrosia artemisiifolia
dust mites
plant pathogenic bacteria
Cryptomeria japonica
arts
enzymes
cross reaction
standardization
Austria
Hungary
pectins

Cite this

Schmidt, G., Wopfner, N., Ferreira, F., & Ritala, A. (2007). Recombinant Amb a 1 expression. In Plants for Human Health in the Post-Genome Era: PSE Congress (pp. 125-125). [E1] Espoo: VTT Technical Research Centre of Finland. VTT Symposium, No. 249
Schmidt, Georg ; Wopfner, N. ; Ferreira, F. ; Ritala, Anneli. / Recombinant Amb a 1 expression. Plants for Human Health in the Post-Genome Era: PSE Congress. Espoo : VTT Technical Research Centre of Finland, 2007. pp. 125-125 (VTT Symposium; No. 249).
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abstract = "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.",
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Schmidt, G, Wopfner, N, Ferreira, F & Ritala, A 2007, Recombinant Amb a 1 expression. in Plants for Human Health in the Post-Genome Era: PSE Congress., E1, VTT Technical Research Centre of Finland, Espoo, VTT Symposium, no. 249, pp. 125-125, PSE Congress: Plants for Human Health in the Post-Genome Era, Helsinki, Finland, 26/08/07.

Recombinant Amb a 1 expression. / Schmidt, Georg; Wopfner, N.; Ferreira, F.; Ritala, Anneli.

Plants for Human Health in the Post-Genome Era: PSE Congress. Espoo : VTT Technical Research Centre of Finland, 2007. p. 125-125 E1 (VTT Symposium; No. 249).

Research output: Chapter in Book/Report/Conference proceedingConference abstract in proceedingsScientific

TY - CHAP

T1 - Recombinant Amb a 1 expression

AU - Schmidt, Georg

AU - Wopfner, N.

AU - Ferreira, F.

AU - Ritala, Anneli

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

M3 - Conference abstract in proceedings

SN - 978-951-38-6321-0

T3 - VTT Symposium

SP - 125

EP - 125

BT - Plants for Human Health in the Post-Genome Era

PB - VTT Technical Research Centre of Finland

CY - Espoo

ER -

Schmidt G, Wopfner N, Ferreira F, Ritala A. Recombinant Amb a 1 expression. In Plants for Human Health in the Post-Genome Era: PSE Congress. Espoo: VTT Technical Research Centre of Finland. 2007. p. 125-125. E1. (VTT Symposium; No. 249).