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

Journal Article · · Journal of Biological Chemistry
 [1];  [2];  [2];  [3];  [2];  [2];  [2];  [4];  [2]
  1. Univ. of South Carolina, Columbia, SC (United States); Davidson College, NC (United States)
  2. Univ. of South Carolina, Columbia, SC (United States)
  3. Univ. of Virginia, Charlottesville, VA (United States)
  4. Medical Univ. of Bialystok (Poland)
+ Show Author Affiliations

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.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institute of Allergy and Infectious Diseases (NIAID); National Institutes of Health (NIH); Medical University of Bialystok
Grant/Contract Number:
W-31-109-ENG-38; R01AI077653
OSTI ID:
1314252
Journal Information:
Journal of Biological Chemistry, Vol. 291, Issue 30; ISSN 0021-9258
Publisher:
American Society for Biochemistry and Molecular BiologyCopyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 27 works
Citation information provided by
Web of Science

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Cited By (9)

Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis journal November 2016
Ragweed Pollen Allergy: Burden, Characteristics, and Management of an Imported Allergen Source in Europe journal January 2018
Molecular approach to a patient’s tailored diagnosis of the oral allergy syndrome journal June 2020
A robust method for the estimation and visualization of IgE cross-reactivity likelihood between allergens belonging to the same protein family journal November 2018
Analysis of Pollen Allergens in Lily by Transcriptome and Proteome Data journal November 2019
Production and Use of Recombinant Profilins Amb a 8, Art v 4, Bet v 2, and Phl p 12 for Allergenic Sensitization Studies journal January 2020
Impact of an N-terminal Polyhistidine Tag on Protein Thermal Stability journal January 2018
Structural insights into the IgE mediated responses induced by the allergens Hev b 8 and Zea m 12 in their dimeric forms journal September 2016
Mugwort Pollen-Related Food Allergy: Lipid Transfer Protein Sensitization and Correlation With the Severity of Allergic Reactions in a Chinese Population journal January 2019

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
allergen
allergy
crystal structure
epitope
mapping
protein stability
IgE binding
peptide binding
pollen