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Membranes
Special Issues
Lipid Binding and Transfer Proteins
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Lipid Binding and Transfer Proteins

A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membrane Functions".

Deadline for manuscript submissions: closed (31 October 2021) | Viewed by 6221

Special Issue Editor

Dr. Ekaterina I. Finkina

E-Mail Website
Guest Editor
M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia
Interests: plant innate immunity; plant pathogenesis related proteins (PR-proteins); lipid transfer proteins (LTPs); defensins; Bet v 1 homologues; lipid binding; antimicrobial activity; membrane permeability; recombinant expression of proteins; plant allergens; allergy; sensitization
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Lipid binding and transfer proteins have been isolated from bacteria, plants, yeasts, and mammals, including humans. These proteins are able to interact with lipid ligands due to the presence of hydrophobic pockets, hydrophobic cavities, or specialized domains in their structure. These proteins carry out the extracellular and intracellular transport of a wide range of hydrophobic molecules, including fatty acids, phospho-, glyco- and sphingolipids, sterols, as well as different secondary metabolites. As a result, they are involved in a variety of processes in living organisms such as lipid metabolism, signal transduction, autophagy, endocytosis, membrane transport, and stress protection, among others. The aim of this Special Issue is to bring together manuscripts devoted to the study of the diversity and structural features of these proteins, the mechanisms of binding and transfer of hydrophobic ligands, as well as their important physiological role and possible application in various spheres of human life. Reviews, short communications, and original research articles are invited for publication. We are eager to receive your submissions to this Special Issue.

Dr. Ekaterina I. Finkina
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Membranes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • lipid transfer protein
  • protein structure
  • molecular dynamics
  • lipid binding
  • hydrophobic ligand
  • mechanisms of binding and transfer of hydrophobic ligands
  • lipid metabolism
  • signal transduction
  • membrane transport
  • plant protection
  • human health
  • protein application

Published Papers (3 papers)

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Research

13 pages, 3102 KiB  
Article
Effect of Point Mutations on Structural and Allergenic Properties of the Lentil Allergen Len c 3
by Daria N. Melnikova, Ekaterina I. Finkina, Ivan V. Bogdanov, Anastasia A. Ignatova, Natalia S. Matveevskaya, Andrey A. Tagaev and Tatiana V. Ovchinnikova
Membranes 2021, 11(12), 939; https://doi.org/10.3390/membranes11120939 - 27 Nov 2021
Cited by 4 | Viewed by 1495
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Lipid Binding and Transfer Proteins)
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13 pages, 3782 KiB  
Article
Effects of Salinity and Abscisic Acid on Lipid Transfer Protein Accumulation, Suberin Deposition and Hydraulic Conductance in Pea Roots
by Guzel R. Akhiyarova, Ruslan S. Ivanov, Igor I. Ivanov, Ekaterina I. Finkina, Daria N. Melnikova, Ivan V. Bogdanov, Tatyana Nuzhnaya, Tatiana V. Ovchinnikova, Dmitriy S. Veselov and Guzel R. Kudoyarova
Membranes 2021, 11(10), 762; https://doi.org/10.3390/membranes11100762 - 1 Oct 2021
Cited by 8 | Viewed by 2221
Abstract
Lipid transfer proteins (LTPs) participate in many important physiological processes in plants, including adaptation to stressors, e.g., salinity. Here we address the mechanism of this protective action of LTPs by studying the interaction between LTPs and abscisic acid (ABA, a “stress” hormone) and [...] Read more.
Lipid transfer proteins (LTPs) participate in many important physiological processes in plants, including adaptation to stressors, e.g., salinity. Here we address the mechanism of this protective action of LTPs by studying the interaction between LTPs and abscisic acid (ABA, a “stress” hormone) and their mutual participation in suberin deposition in root endodermis of salt-stressed pea plants. Using immunohistochemistry we show for the first time NaCl induced accumulation of LTPs and ABA in the cell walls of phloem paralleled by suberin deposition in the endoderm region of pea roots. Unlike LTPs which were found localized around phloem cells, ABA was also present within phloem cells. In addition, ABA treatment resulted in both LTP and ABA accumulation in phloem cells and promoted root suberization. These results suggested the importance of NaCl-induced accumulation of ABA in increasing the abundance of LTPs and of suberin. Using molecular modeling and fluorescence spectroscopy we confirmed the ability of different plant LTPs, including pea Ps-LTP1, to bind ABA. We therefore hypothesize an involvement of plant LTPs in ABA transport (unloading from phloem) as part of the salinity adaptation mechanism. Full article
(This article belongs to the Special Issue Lipid Binding and Transfer Proteins)
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12 pages, 2465 KiB  
Article
Do Lipids Influence Gastrointestinal Processing: A Case Study of Major Soybean Allergen Gly m 4
by Ekaterina I. Finkina, Daria N. Melnikova, Ivan V. Bogdanov, Anastasia A. Ignatova and Tatiana V. Ovchinnikova
Membranes 2021, 11(10), 754; https://doi.org/10.3390/membranes11100754 - 30 Sep 2021
Cited by 2 | Viewed by 1797
Abstract
Previously, we have demonstrated that Gly m 4, one of the major soybean allergens, could pass through the Caco-2 epithelial barrier and have proposed a mechanism of sensitization. However, it is not known yet whether Gly m 4 can reach the intestine in [...] Read more.
Previously, we have demonstrated that Gly m 4, one of the major soybean allergens, could pass through the Caco-2 epithelial barrier and have proposed a mechanism of sensitization. However, it is not known yet whether Gly m 4 can reach the intestine in its intact form after digestion in stomach. In the present work, we studied an influence of various factors including lipids (fatty acids and lysolipids) on digestibility of Gly m 4. Using fluorescent and CD spectroscopies, we showed that Gly m 4 interacted with oleic acid and LPPG (lyso-palmitoyl phosphatidylglycerol), but its binding affinity greatly decreased under acidic conditions, probably due to the protein denaturation. The mimicking of gastric digestion revealed that Gly m 4 digestibility could be significantly reduced with the change of pH value and pepsin-to-allergen ratio, as well as by the presence of LPPG. We suggested that the protective effect of LPPG was unlikely associated with the allergen binding, but rather connected to the pepsin inhibition due to the lipid interaction with its catalytic site. As a result, we assumed that, under certain conditions, the intact Gly m 4 might be able to reach the human intestine and thereby could be responsible for allergic sensitization. Full article
(This article belongs to the Special Issue Lipid Binding and Transfer Proteins)
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