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Solution structure, copper binding and backbone dynamics of recombinant Ber e 1: the major allergen from brazil nut
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
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2012 (Engelska)Ingår i: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 7, nr 10, s. e46435-Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

BACKGROUND: The 2S albumin Ber e 1 is the major allergen in Brazil nuts. Previous findings indicated that the protein alone does not cause an allergenic response in mice, but the addition of components from a Brazil nut lipid fraction were required. Structural details of Ber e 1 may contribute to the understanding of the allergenic properties of the protein and its potential interaction partners. METHODOLOGY/PRINCIPAL FINDINGS: The solution structure of recombinant Ber e 1 was solved using NMR spectroscopy and measurements of the protein back bone dynamics at a residue-specific level were extracted using (15)N-spin relaxation. A hydrophobic cavity was identified in the structure of Ber e 1. Using the paramagnetic relaxation enhancement property of Cu(2+) in conjunction with NMR, it was shown that Ber e 1 is able to specifically interact with the divalent copper ion and the binding site was modeled into the structure. The IgE binding region as well as the copper binding site show increased dynamics on both fast ps-ns timescale as well as slower µs-ms timescale. CONCLUSIONS/SIGNIFICANCE: The overall fold of Ber e 1 is similar to other 2S albumins, but the hydrophobic cavity resembles that of a homologous non-specific lipid transfer protein. Ber e 1 is the first 2S albumin shown to interact with Cu(2+) ions. This Cu(2+) binding has minimal effect on the electrostatic potential on the surface of the protein, but the charge distribution within the hydrophobic cavity is significantly altered. As the hydrophobic cavity is likely to be involved in a putative lipid interaction the Cu(2+) can in turn affect the interaction that is essential to provoke an allergenic response.

Ort, förlag, år, upplaga, sidor
San Francisco: Public Library of Science , 2012. Vol. 7, nr 10, s. e46435-
Nationell ämneskategori
Kemi
Identifikatorer
URN: urn:nbn:se:umu:diva-60707DOI: 10.1371/journal.pone.0046435ISI: 000309580800019PubMedID: 23056307OAI: oai:DiVA.org:umu-60707DiVA, id: diva2:562168
Tillgänglig från: 2012-10-29 Skapad: 2012-10-23 Senast uppdaterad: 2018-06-08Bibliografiskt granskad
Ingår i avhandling
1. Thermodynamical and structural properties of proteins and their role in food allergy
Öppna denna publikation i ny flik eller fönster >>Thermodynamical and structural properties of proteins and their role in food allergy
2013 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]

Proteins are important building blocks of all living organisms. They are composed of a defined sequence of different amino acids, and fold into a specific three-dimensional, ordered structure. The three-dimensional structure largely determines the function of the protein, but protein function always requires motion. Small movements within the protein structure govern the functional properties, and this thesis aims to better understand these discrete protein movements. The motions within the protein structure are governed by thermodynamics, which therefore is useful to predict protein interactions.

Nuclear magnetic resonance (NMR) is a powerful tool to study proteins at atomic resolution. Therefore, NMR is the primary method used within this thesis, along with other biophysical techniques such as Fluorescence spectroscopy, Circular Dichroism spectroscopy and in silico modeling.

In paper I, NMR in combination with molecular engineering is used to show that the folding of the catalytical subdomains of the enzyme Adenylate kinase does not affect the core of the protein, and thus takes a first step to linking folding, thermodynamic stability and catalysis.

In paper II, the structure of the primary allergen from Brazil nut, Ber e 1, is presented along with biophysical measurements that help explain the allergenic potential of the protein.

Paper III describes the need for a specific Brazil nut lipid fraction needed to induce an allergenic response. NMR and fluorescence spectroscopy is used to show that there is a direct interaction between Ber e 1 and one or several components in the lipid fraction.

Ort, förlag, år, upplaga, sidor
Umeå: Umeå universitet, 2013. s. 33
Serie
Umeå University medical dissertations, ISSN 0346-6612 ; 1571
Nyckelord
Protein folding, NMR, Food allergy, allergen, protein interactions
Nationell ämneskategori
Biofysik Strukturbiologi Biokemi och molekylärbiologi Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)
Forskningsämne
medicinsk biokemi
Identifikatorer
urn:nbn:se:umu:diva-68020 (URN)978-91-7459-613-7 (ISBN)
Disputation
2013-05-03, KB3A9, plan 3, KBC-huset, Umeå Universitet, Umeå, 09:00 (Engelska)
Opponent
Handledare
Tillgänglig från: 2013-04-12 Skapad: 2013-04-10 Senast uppdaterad: 2018-06-08Bibliografiskt granskad

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