TY - JOUR
T1 - Nitration of the Birch Pollen Allergen Bet v 1.0101: Efficiency and Site-Selectivity of Liquid and Gaseous Nitrating Agents
AU - Reinmuth-Selzle, K.
AU - Ackaert, C.
AU - Kampf, C.J.
AU - Samonig, M.
AU - Shiraiwa, M.
AU - Kofler, S.
AU - Yang, H.
AU - Gadermaier, G.
AU - Brandstetter, H.
AU - Huber, C.G.
AU - Duschl, A.
AU - Oostingh, G.J.
AU - Pöschl, U.
N1 - Cited By :45
Export Date: 14 December 2023
CODEN: JPROB
Correspondence Address: Pöschl, U.; Multiphase Chemistry and Biogeochemistry Departments, Hahn-Meitner Weg 1, 55128 Mainz, Germany; email: [email protected]
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PY - 2014
Y1 - 2014
N2 - Nitration of the major birch pollen allergen Bet v 1 alters the immune responses toward this protein, but the underlying chemical mechanisms are not yet understood. Here we address the efficiency and site-selectivity of the nitration reaction of recombinant protein samples of Bet v 1.0101 with different nitrating agents relevant for laboratory investigations (tetranitromethane, TNM), for physiological processes (peroxynitrite, ONOO-), and for the health effects of environmental pollutants (nitrogen dioxide and ozone, O 3/NO2). We determined the total tyrosine nitration degrees (ND) and the NDs of individual tyrosine residues (NDY). High-performance liquid chromatography coupled to diode array detection and HPLC coupled to high-resolution mass spectrometry analysis of intact proteins, HPLC coupled to tandem mass spectrometry analysis of tryptic peptides, and amino acid analysis of hydrolyzed samples were performed. The preferred reaction sites were tyrosine residues at the following positions in the polypeptide chain: Y83 and Y81 for TNM, Y150 for ONOO-, and Y83 and Y158 for O 3/NO2. The tyrosine residues Y83 and Y81 are located in a hydrophobic cavity, while Y150 and Y158 are located in solvent-accessible and flexible structures of the C-terminal region. The heterogeneous reaction with O3/NO2 was found to be strongly dependent on the phase state of the protein. Nitration rates were about one order of magnitude higher for aqueous protein solutions (∼20% per day) than for protein filter samples (∼2% per day). Overall, our findings show that the kinetics and site-selectivity of nitration strongly depend on the nitrating agent and reaction conditions, which may also affect the biological function and adverse health effects of the nitrated protein. © 2014 American Chemical Society.
AB - Nitration of the major birch pollen allergen Bet v 1 alters the immune responses toward this protein, but the underlying chemical mechanisms are not yet understood. Here we address the efficiency and site-selectivity of the nitration reaction of recombinant protein samples of Bet v 1.0101 with different nitrating agents relevant for laboratory investigations (tetranitromethane, TNM), for physiological processes (peroxynitrite, ONOO-), and for the health effects of environmental pollutants (nitrogen dioxide and ozone, O 3/NO2). We determined the total tyrosine nitration degrees (ND) and the NDs of individual tyrosine residues (NDY). High-performance liquid chromatography coupled to diode array detection and HPLC coupled to high-resolution mass spectrometry analysis of intact proteins, HPLC coupled to tandem mass spectrometry analysis of tryptic peptides, and amino acid analysis of hydrolyzed samples were performed. The preferred reaction sites were tyrosine residues at the following positions in the polypeptide chain: Y83 and Y81 for TNM, Y150 for ONOO-, and Y83 and Y158 for O 3/NO2. The tyrosine residues Y83 and Y81 are located in a hydrophobic cavity, while Y150 and Y158 are located in solvent-accessible and flexible structures of the C-terminal region. The heterogeneous reaction with O3/NO2 was found to be strongly dependent on the phase state of the protein. Nitration rates were about one order of magnitude higher for aqueous protein solutions (∼20% per day) than for protein filter samples (∼2% per day). Overall, our findings show that the kinetics and site-selectivity of nitration strongly depend on the nitrating agent and reaction conditions, which may also affect the biological function and adverse health effects of the nitrated protein. © 2014 American Chemical Society.
KW - air pollution
KW - Bet v 1.0101
KW - HPLC-MS/MS
KW - nitration sites
KW - tyrosine nitration
KW - pollen antigen
KW - polypeptide
KW - amino acid analysis
KW - article
KW - birch
KW - high performance liquid chromatography
KW - liquid chromatography
KW - mass spectrometry
KW - nitration
KW - pollutant
KW - priority journal
KW - tandem mass spectrometry
KW - Amino Acid Sequence
KW - Antigens, Plant
KW - Betula
KW - Escherichia coli
KW - Gene Expression
KW - Kinetics
KW - Models, Molecular
KW - Molecular Sequence Data
KW - Nitrogen Dioxide
KW - Ozone
KW - Peptides
KW - Peroxynitrous Acid
KW - Pollen
KW - Protein Structure, Secondary
KW - Recombinant Proteins
KW - Tetranitromethane
KW - Tyrosine
U2 - 10.1021/pr401078h
DO - 10.1021/pr401078h
M3 - Article
SN - 1535-3893
VL - 13
SP - 1570
EP - 1577
JO - Journal of Proteome Research
JF - Journal of Proteome Research
IS - 3
ER -