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Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3
Plant lipid transfer proteins (LTPs) are known to be clinically significant allergens capable of binding various lipid ligands. Recent data showed that lipid ligands affected the allergenic properties of plant LTPs. In this work, we checked the assumption that specific amino acid residues in the Len...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8703665/ https://www.ncbi.nlm.nih.gov/pubmed/34940440 http://dx.doi.org/10.3390/membranes11120939 |
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author | Melnikova, Daria N. Finkina, Ekaterina I. Bogdanov, Ivan V. Ignatova, Anastasia A. Matveevskaya, Natalia S. Tagaev, Andrey A. Ovchinnikova, Tatiana V. |
author_facet | Melnikova, Daria N. Finkina, Ekaterina I. Bogdanov, Ivan V. Ignatova, Anastasia A. Matveevskaya, Natalia S. Tagaev, Andrey A. Ovchinnikova, Tatiana V. |
author_sort | Melnikova, Daria N. |
collection | PubMed |
description | Plant lipid transfer proteins (LTPs) are known to be clinically significant allergens capable of binding various lipid ligands. Recent data showed that lipid ligands affected the allergenic properties of plant LTPs. In this work, we checked the assumption that specific amino acid residues in the Len c 3 structure can play a key role both in the interaction with lipid ligands and IgE-binding capacity of the allergen. The recombinant analogues of Len c 3 with the single or double substitutions of Thr41, Arg45 and/or Tyr80 were obtained by site-directed mutagenesis. All these amino acid residues are located near the “bottom” entrance to the hydrophobic cavity of Len c 3 and are likely included in the IgE-binding epitope of the allergen. Using a bioinformatic approach, circular dichroism and fluorescence spectroscopies, ELISA, and experiments mimicking the allergen Len c 3 gastroduodenal digestion we showed that the substitution of all the three amino acid residues significantly affected structural organization of this region and led both to a change of the ligand-binding capacity and the allergenic potential of Len c 3. |
format | Online Article Text |
id | pubmed-8703665 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87036652021-12-25 Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3 Melnikova, Daria N. Finkina, Ekaterina I. Bogdanov, Ivan V. Ignatova, Anastasia A. Matveevskaya, Natalia S. Tagaev, Andrey A. Ovchinnikova, Tatiana V. Membranes (Basel) Article Plant lipid transfer proteins (LTPs) are known to be clinically significant allergens capable of binding various lipid ligands. Recent data showed that lipid ligands affected the allergenic properties of plant LTPs. In this work, we checked the assumption that specific amino acid residues in the Len c 3 structure can play a key role both in the interaction with lipid ligands and IgE-binding capacity of the allergen. The recombinant analogues of Len c 3 with the single or double substitutions of Thr41, Arg45 and/or Tyr80 were obtained by site-directed mutagenesis. All these amino acid residues are located near the “bottom” entrance to the hydrophobic cavity of Len c 3 and are likely included in the IgE-binding epitope of the allergen. Using a bioinformatic approach, circular dichroism and fluorescence spectroscopies, ELISA, and experiments mimicking the allergen Len c 3 gastroduodenal digestion we showed that the substitution of all the three amino acid residues significantly affected structural organization of this region and led both to a change of the ligand-binding capacity and the allergenic potential of Len c 3. MDPI 2021-11-27 /pmc/articles/PMC8703665/ /pubmed/34940440 http://dx.doi.org/10.3390/membranes11120939 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Melnikova, Daria N. Finkina, Ekaterina I. Bogdanov, Ivan V. Ignatova, Anastasia A. Matveevskaya, Natalia S. Tagaev, Andrey A. Ovchinnikova, Tatiana V. Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3 |
title | Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3 |
title_full | Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3 |
title_fullStr | Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3 |
title_full_unstemmed | Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3 |
title_short | Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3 |
title_sort | effect of point mutations on structural and allergenic properties of the lentil allergen len c 3 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8703665/ https://www.ncbi.nlm.nih.gov/pubmed/34940440 http://dx.doi.org/10.3390/membranes11120939 |
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