title: Structural, Functional, and Immunological Characterization of Profilin Panallergens Amb a 8, Art v 4, and Bet v 2.
abstract: Ragweed allergens affect several million people in the United States and Canada. To date, only two ragweed allergens, Amb t 5 and Amb a 11, have their structures determined and deposited to the Protein Data Bank. Here, we present structures of methylated ragweed allergen Amb a 8, Amb a 8 in the presence of poly(l-proline), and Art v 4 (mugwort allergen). Amb a 8 and Art v 4 are panallergens belonging to the profilin family of proteins. They share significant sequence and structural similarities, which results in cross-recognition by IgE antibodies. Molecular and immunological properties of Amb a 8 and Art v 4 are compared with those of Bet v 2 (birch pollen allergen) as well as with other allergenic profilins. We purified recombinant allergens that are recognized by patient IgE and are highly cross-reactive. It was determined that the analyzed allergens are relatively unstable. Structures of Amb a 8 in complex with poly(l-proline)10 or poly(l-proline)14 are the first structures of the plant profilin in complex with proline-rich peptides. Amb a 8 binds the poly(l-proline) in a mode similar to that observed in human, mouse, and P. falciparum profilin·peptide complexes. However, only some of the residues that form the peptide binding site are conserved.
authors.affiliation: From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, the Department of Chemistry, Davidson College, Davidson, North Carolina 28035.
authors.forename: Lesa R
authors.initials: LR
authors.lastname: Offermann
authors.affiliation: From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208.
authors.forename: Caleb R
authors.initials: CR
authors.lastname: Schlachter
authors.affiliation: From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208.
authors.forename: Makenzie L
authors.initials: ML
authors.lastname: Perdue
authors.affiliation: the Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908, and.
authors.forename: Karolina A
authors.initials: KA
authors.lastname: Majorek
authors.affiliation: From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208.
authors.forename: John Z
authors.initials: JZ
authors.lastname: He
authors.affiliation: From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208.
authors.forename: William T
authors.initials: WT
authors.lastname: Booth
authors.affiliation: From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208.
authors.forename: Jessica
authors.initials: J
authors.lastname: Garrett
authors.affiliation: the Departments of Allergology and Internal Medicine and Experimental Allergology and Immunology, Medical University of Bialystok, Bialystok 15-276, Poland.
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Kowal
authors.affiliation: From the Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, chruszcz@mailbox.sc.edu.
authors.forename: Maksymilian
authors.initials: M
authors.lastname: Chruszcz
mesh_terms: D000818:Animals; D052179:Antigens, Plant / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D003429:Cross Reactions; D006801:Humans; D007073:Immunoglobulin E / Q000737:chemistry* / Q000276:immunology; D051379:Mice; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology
chemical_list: D052179:Antigens, Plant; C526439:Art v 4 allergen, Artemisia vulgaris; C530739:BETV2 protein, Betula pendula; D011994:Recombinant Proteins; D007073:Immunoglobulin E
keywords: IgE binding; allergen; allergy; crystal structure; epitope mapping; peptide binding; pollen; protein stability