Structural and Functional Characterization of the Major Allergen Amb a 11 from Short Ragweed Pollen*
| العنوان: | Structural and Functional Characterization of the Major Allergen Amb a 11 from Short Ragweed Pollen* |
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| المؤلفون: | David Kopečný, Pierre Briozzo, Franck Jagic, Philippe Moingeon, Véronique Bordas-Le Floch, Sabi Airouche, Rachel Groeme, Judith Jaekel, Laurent Mascarell, Laetitia Bussières, Petra Zieglmayer, Maxime Le Mignon, Martin Savko, Nathalie Berjont, Véronique Baron-Bodo |
| المساهمون: | Stallergenes Greer (France, Antony), Palacky University Olomouc, Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Stallergenes, Convention Industrielles de Formation par la Recherche (CIFRE) fellowship from the Association Nationale de la Recherche et de la Technologie, National Program of Sustainability I Grant from the Czech Ministry of Education, Youth and Sports [LO1204], Moingeon, Philippe |
| المصدر: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2016, 291, pp.13076--87. ⟨10.1074/jbc.M115.702001⟩ Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2016, 291 (25), pp.13076--87. ⟨10.1074/jbc.M115.702001⟩ Journal of Biological Chemistry 25 (291), 13076-13087. (2016) |
| بيانات النشر: | American Society for Biochemistry and Molecular Biology, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, Models, Molecular, [SDV]Life Sciences [q-bio], medicine.disease_cause, Crystallography, X-Ray, Biochemistry, law.invention, Mice, 0302 clinical medicine, Allergen, law, Models, Cysteine Proteases, Catalytic Domain, Ambrosia artemisiifolia, Inbred BALB C, Conserved Sequence, Rhinitis, Plant Proteins, chemistry.chemical_classification, Cysteine Proteases/*chemistry/immunology, Plant/*immunology, Enzyme Precursors, Mice, Inbred BALB C, Crystallography, biology, Enzyme Precursors/*chemistry/immunology, Cysteine protease, 3. Good health, Protein Structure and Folding, Recombinant DNA, Female, Ragweed, Molecular Sequence Data, 03 medical and health sciences, Allergic, Catalytic triad, medicine, Animals, Amino Acid Sequence, Antigens, Protein precursor, Molecular Biology, Protein Processing, Plant Extracts, Post-Translational, Molecular, Rhinitis, Allergic, Seasonal, Plant Extracts/*immunology, Hydrogen Bonding, Cell Biology, Plant Proteins/*chemistry/immunology, Allergens, Antigens, Plant, biology.organism_classification, Seasonal/*immunology/prevention & control, Allergens/chemistry/immunology, 030104 developmental biology, Enzyme, 030228 respiratory system, chemistry, Immunology, Proteolysis, X-Ray, Protein Processing, Post-Translational |
| الوصف: | International audience; Allergy to the short ragweed (Ambrosia artemisiifolia) pollen is a major health problem. The ragweed allergen repertoire has been recently expanded with the identification of Amb a 11, a new major allergen belonging to the cysteine protease family. To better characterize Amb a 11, a recombinant proform of the molecule with a preserved active site was produced in Escherichia coli, refolded, and processed in vitro into a mature enzyme. The enzymatic activity is revealed by maturation following an autocatalytic processing resulting in the cleavage of both N- and C-terminal propeptides. The 2.05-A resolution crystal structure of pro-Amb a 11 shows an overall typical C1A cysteine protease fold with a network of molecular interactions between the N-terminal propeptide and the catalytic triad of the enzyme. The allergenicity of Amb a 11 was confirmed in a murine sensitization model, resulting in airway inflammation, production of serum IgEs, and induction of Th2 immune responses. Of note, inflammatory responses were higher with the mature form, demonstrating that the cysteine protease activity critically contributes to the allergenicity of the molecule. Collectively, our results clearly demonstrate that Amb a 11 is a bona fide cysteine protease exhibiting a strong allergenicity. As such, it should be considered as an important molecule for diagnosis and immunotherapy of ragweed pollen allergy. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.M115.702001⟩ |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79e4e206a517c3346f0504160681088a https://europepmc.org/articles/PMC4933224/ |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....79e4e206a517c3346f0504160681088a |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00219258 1083351X |
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| DOI: | 10.1074/jbc.M115.702001⟩ |