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Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein

The recombinant isoforms Lc-LTP1 and Lc-LTP3 of the lentil lipid transfer protein were overexpressed in E. coli cells. It was confirmed that both proteins are stabilized by four disulfide bonds and characterized by a high proportion of the α-helical structure. It was found that Lc-LTP1 and Lc-LTP3 p...

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Autores principales: Bogdanov, I. V., Finkina, E. I., Balandin, S. V., Melnikova, D. N., Stukacheva, E. A., Ovchinnikova, T. V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4610166/
https://www.ncbi.nlm.nih.gov/pubmed/26483961
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author Bogdanov, I. V.
Finkina, E. I.
Balandin, S. V.
Melnikova, D. N.
Stukacheva, E. A.
Ovchinnikova, T. V.
author_facet Bogdanov, I. V.
Finkina, E. I.
Balandin, S. V.
Melnikova, D. N.
Stukacheva, E. A.
Ovchinnikova, T. V.
author_sort Bogdanov, I. V.
collection PubMed
description The recombinant isoforms Lc-LTP1 and Lc-LTP3 of the lentil lipid transfer protein were overexpressed in E. coli cells. It was confirmed that both proteins are stabilized by four disulfide bonds and characterized by a high proportion of the α-helical structure. It was found that Lc-LTP1 and Lc-LTP3 possess antimicrobial activity and can bind fatty acids. Both isoforms have the ability to bind specific IgE from sera of patients with food allergies, which recognize similar epitopes of the major peach allergen Pru p 3. Both isoforms were shown to have immunological properties similar to those of other plant allergenic LTPs, but Lc-LTP3 displayed a less pronounced immunoreactivity.
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spelling pubmed-46101662015-10-19 Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein Bogdanov, I. V. Finkina, E. I. Balandin, S. V. Melnikova, D. N. Stukacheva, E. A. Ovchinnikova, T. V. Acta Naturae Research Article The recombinant isoforms Lc-LTP1 and Lc-LTP3 of the lentil lipid transfer protein were overexpressed in E. coli cells. It was confirmed that both proteins are stabilized by four disulfide bonds and characterized by a high proportion of the α-helical structure. It was found that Lc-LTP1 and Lc-LTP3 possess antimicrobial activity and can bind fatty acids. Both isoforms have the ability to bind specific IgE from sera of patients with food allergies, which recognize similar epitopes of the major peach allergen Pru p 3. Both isoforms were shown to have immunological properties similar to those of other plant allergenic LTPs, but Lc-LTP3 displayed a less pronounced immunoreactivity. A.I. Gordeyev 2015 /pmc/articles/PMC4610166/ /pubmed/26483961 Text en Copyright ® 2015 Park-media Ltd. http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Bogdanov, I. V.
Finkina, E. I.
Balandin, S. V.
Melnikova, D. N.
Stukacheva, E. A.
Ovchinnikova, T. V.
Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein
title Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein
title_full Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein
title_fullStr Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein
title_full_unstemmed Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein
title_short Structural and Functional Characterization of Recombinant Isoforms of the Lentil Lipid Transfer Protein
title_sort structural and functional characterization of recombinant isoforms of the lentil lipid transfer protein
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4610166/
https://www.ncbi.nlm.nih.gov/pubmed/26483961
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