Structural, Functional, and Immunological Characterization of Profilin Panallergens Amb a 8, Art v 4, and Bet v 2

Offermann, Lesa R.; Schlachter, Caleb R.; Perdue, Makenzie L.; Majorek, Karolina A.; He, John Z.; Booth, William T.; Garrett, Jessica; Kowal, Krzysztof; Chruszcz, Maksymilian

doi:10.1074/jbc.m116.733659

Structural, Functional, and Immunological Characterization of Profilin Panallergens Amb a 8, Art v 4, and Bet v 2

Journal Article · Thu May 26 00:00:00 EDT 2016 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.m116.733659· OSTI ID:1314252

Offermann, Lesa R. ^[1]; Schlachter, Caleb R. ^[2]; Perdue, Makenzie L. ^[2]; Majorek, Karolina A. ^[3]; He, John Z. ^[2]; Booth, William T. ^[2]; Garrett, Jessica ^[2]; Kowal, Krzysztof ^[4]; Chruszcz, Maksymilian ^[2]

Univ. of South Carolina, Columbia, SC (United States); Davidson College, NC (United States)
Univ. of South Carolina, Columbia, SC (United States)
Univ. of Virginia, Charlottesville, VA (United States)
Medical Univ. of Bialystok (Poland)

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. In this paper, 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.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: Medical University of Bialystok; National Institute of Allergy and Infectious Diseases (NIAID); National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: W-31109-ENG-38

OSTI ID:: 1314252

Journal Information:: Journal of Biological Chemistry, Journal Name: Journal of Biological Chemistry Journal Issue: 30 Vol. 291; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Structural, Functional, and Immunological Characterization of Profilin Panallergens Amb a 8, Art v 4, and Bet v 2

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