Expression of the major mugwort pollen allergen Art v 1 in tobacco plants and cell cultures: problems and perspectives for allergen production in plants

Siegert, Marc; Pertl-Obermeyer, Heidi; Gadermaier, Gabriele; Ferreira, Fátima; Obermeyer, Gerhard

doi:10.1007/s00299-011-1199-3

Cited by 7 publications

(4 citation statements)

References 43 publications

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“…Plants are also attractive platforms for producing allergens, both because many allergens are of plant origin and because they provide an inexpensive scalable system that is not prone to infection by human pathogens (Schmidt et al ., ). Nicotiana benthamiana , a well‐established tobacco system, has been used to make allergens from birch pollen (Krebitz et al ., ), mugwort pollen (Siegert et al ., ) and apple (Krebitz et al ., ). Hypoallergenic birch pollen allergens were recently made in rice (Ogo et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Immunotherapy using algal‐produced Ara h 1 core domain suppresses peanut allergy in mice

Gregory

Shepley-McTaggart

Umpierrez

et al. 2016

Plant Biotechnology Journal

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SummaryPeanut allergy is an IgE‐mediated adverse reaction to a subset of proteins found in peanuts. Immunotherapy aims to desensitize allergic patients through repeated and escalating exposures for several months to years using extracts or flours. The complex mix of proteins and variability between preparations complicates immunotherapy studies. Moreover, peanut immunotherapy is associated with frequent negative side effects and patients are often at risk of allergic reactions once immunotherapy is discontinued. Allergen‐specific approaches using recombinant proteins are an attractive alternative because they allow more precise dosing and the opportunity to engineer proteins with improved safety profiles. We tested whether Ara h 1 and Ara h 2, two major peanut allergens, could be produced using chloroplast of the unicellular eukaryotic alga, Chlamydomonas reinhardtii. C. reinhardtii is novel host for producing allergens that is genetically tractable, inexpensive and easy to grow, and is able to produce more complex proteins than bacterial hosts. Compared to the native proteins, algal‐produced Ara h 1 core domain and Ara h 2 have a reduced affinity for IgE from peanut‐allergic patients. We further found that immunotherapy using algal‐produced Ara h 1 core domain confers protection from peanut‐induced anaphylaxis in a murine model of peanut allergy.

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Section: Introductionmentioning

confidence: 99%

Immunotherapy using algal‐produced Ara h 1 core domain suppresses peanut allergy in mice

Gregory

Shepley-McTaggart

Umpierrez

et al. 2016

Plant Biotechnology Journal

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“…In Art v 1, the major pollen allergen from mugwort (Artemisia vulgaris) mono arabinosylated Hyp has been shown to react with serum antibodies from allergic patients [33]. While allergenic epitopes must be avoided in recombinant therapeutics, plant-based production systems offer the possibility to produce authentic recombinant allergens [34,35] to facilitate componentresolved diagnosis and subsequent immunotherapy of allergic patients.…”

Section: Glycan Engineeringmentioning

confidence: 99%

Optimizing product quality in molecular farming

Schiermeyer

2020

Current Opinion in Biotechnology

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With a first commercial biopharmaceutical product on the market, and other products proceeding through clinical development stages, the concept of plant molecular farming has proven a viable alternative to traditional production platforms. To extend the range of target molecules amenable for molecular farming, there is constant ambition to tailor the current plant host systems to improve the quality of the final product. These efforts have been focused mainly on glycan engineering, as the majority of target molecules are glycoproteins. In the past few years also more research addressed proteolytic processing of recombinant target molecules and strategies have been devised to protect valuable target proteins from degradation. Recent developments in these areas as well as in downstream processing including extraction and purification processes will be discussed.

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“…However, in the case of plant cells, this situation could change in the next few years, given the increasing interest in developing “ molecular farming ” as a cost-effective alternative for production of pharmaceutical proteins. Plant cell-based systems are easy to scale up for large amounts of low-cost biomass production, having lower risk of protein contamination with human pathogens compared to bacteria, yeast, or mammalian cells [ 98 ]. In addition, plant cells are able to perform full post-translational modifications in the expressed molecule, ensuring proper folding and biological activity [ 99 ].…”

Section: Production Of Recombinant Allergens: From Gene To Proper mentioning

confidence: 99%

Facing Hymenoptera Venom Allergy: From Natural to Recombinant Allergens

Pérez-Riverol

Justo-Jacomini

Zollner

et al. 2015

Toxins

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Along with food and drug allergic reactions, a Hymenoptera insect Sting (Apoidea, Vespidae, Formicidae) is one of the most common causes of anaphylaxis worldwide. Diagnoses of Hymenoptera venom allergy (HVA) and specific immunotherapy (SIT) have been based on the use of crude venom extracts. However, the incidence of cross-reactivity and low levels of sensibility during diagnosis, as well as the occurrence of nonspecific sensitization and undesired side effects during SIT, encourage the search for novel allergenic materials. Recombinant allergens are an interesting approach to improve allergy diagnosis and SIT because they circumvent major problems associated with the use of crude venom. Production of recombinant allergens depends on the profound molecular characterization of the natural counterpart by combining some “omics” approaches with high-throughput screening techniques and the selection of an appropriate system for heterologous expression. To date, several clinically relevant allergens and novel venom toxins have been identified, cloned and characterized, enabling a better understanding of the whole allergenic and envenoming processes. Here, we review recent findings on identification, molecular characterization and recombinant expression of Hymenoptera venom allergens and on the evaluation of these heterologous proteins as valuable tools for tackling remaining pitfalls on HVA diagnosis and immunotherapy.

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Expression of the major mugwort pollen allergen Art v 1 in tobacco plants and cell cultures: problems and perspectives for allergen production in plants

Cited by 7 publications

References 43 publications

Immunotherapy using algal‐produced Ara h 1 core domain suppresses peanut allergy in mice

Immunotherapy using algal‐produced Ara h 1 core domain suppresses peanut allergy in mice

Optimizing product quality in molecular farming

Facing Hymenoptera Venom Allergy: From Natural to Recombinant Allergens

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