Plant non-specific lipid transfer proteins: An overview

Missaoui, Khawla; González-Klein, Zulema; Pazos-Castro, Diego; Hernández-Ramírez, Guadalupe; Garrido‐Arandia, María; Brini, Faïçal; Díaz‐Perales, Araceli; Tomé-Amat, Jaime

doi:10.1016/j.plaphy.2021.12.026

Cited by 58 publications

(47 citation statements)

References 129 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The other conserved pentapeptide T/S-X-X-D-R/K was found to be located at position 67 to 71. Otherwise, by calculating the cavities of both nsLTPs using the DogSite method implemented in the Proteins Plus server the cavity is larger in TdLTP1 than in TdLTP2 (In the case of the TdLTP2 we have found a pocket of 678 amstrong vs 1095 amstrong in the TdLTP1), which has pronounced flexibility allows accommodating bigger ligands with a rigid structure, such as sterols [ 36 ].…”

Section: Discussionmentioning

confidence: 99%

Identification and molecular characterization of a novel non-specific lipid transfer protein (TdLTP2) from durum wheat

et al. 2022

Self Cite

View full text Add to dashboard Cite

Non-specific lipid transfer proteins (nsLTPs) are small, cysteine-rich proteins, a part of the pathogenesis-related protein family, and numerous of them act as positive regulators during plant disease resistance, growth, and reproduction. These proteins are involved also in the intracellular transfer of lipids, as well as in plant immune responses. Besides their differences in sequences, they show similar features in their structure. However, they show distinct lipid-binding specificities signifying their various biological roles that dictate further structural study. This study reports the identification, in silico characterization and purification of a novel member of the nsLTP2 protein family from durum wheat, TdLTP2. It was generated and purified using the combination of gel filtration chromatography and reverse-phase high-performance liquid chromatography (RP-HPLC). Its identity was detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and mass spectrometry (MALDI-TOF). TdLTP2 had been expressed in different stress to detect its localization; therefore, fluor-immunolocalization studies accomplished this data. In this approach, to assess the allergenicity of TdLTP2, thirty patients with baker’s asthma were enrolled and ELISA to detect the presence of specific IgE antibodies tested their sera. Moreover, the lipid-binding properties of TdLTP2 were examined in vitro and validated using a molecular docking study. In summary, our results demonstrate a new addition of member in plant nsLTPs family, TdLTP2, which can develop a better understanding about its biological functions and shed light on future applications.

show abstract

Section: Discussionmentioning

confidence: 99%

Identification and molecular characterization of a novel non-specific lipid transfer protein (TdLTP2) from durum wheat

et al. 2022

Self Cite

View full text Add to dashboard Cite

show abstract

“…Thus, regardless of the obvious advances in immunotherapy treatments ( 24 ), the general recommendation from clinicians is still to avoid the contact with the allergen sources ( 25 ). The molecules in the food responsible for allergy triggering in susceptible individuals are the allergens, most of which are proteins and/or lipoproteins ( 26 – 28 ). Over the last few years, increasing attention is being paid to the application of nanotechnology (nanoparticles) to specific applications such as allergen detection, diagnosis and allergen-specific immunotherapy (AIT) ( 29 – 32 ).…”

Section: Introductionmentioning

confidence: 99%

Suitability of potyviral recombinant virus-like particles bearing a complete food allergen for immunotherapy vaccines

Pazos-Castro

Margain²,

González-Klein³

et al. 2022

Front. Immunol.

Self Cite

View full text Add to dashboard Cite

Virus-like particles (VLPs) have been gaining attention as potential platforms for delivery of cargos in nanomedicine. Although animal viruses are largely selected due to their immunostimulatory capacities, VLPs from plant viruses constitute a promising alternative to be considered. VLPs derived from Turnip mosaic virus (TuMV) have proven to present a tridimensional structure suited to display molecules of interest on their surface, making them interesting tools to be studied in theragnostic strategies. Here, we study their potential in the treatment of food allergy by genetically coupling TuMV-derived VLPs to Pru p 3, one of the most dominant allergens in Mediterranean climates. VLPs-Pru p 3 were generated by cloning a synthetic gene encoding the TuMV coat protein and Pru p 3, separated by a linker, into a transient high-expression vector, followed by agroinfiltration in Nicotiana benthamiana plants. The generated fusion protein self-assembled in planta to form the VLPs, which were purified by exclusion chromatography. Their elongated morphology was confirmed by electron microscopy and their size (~400 nm), and monodispersity was confirmed by dynamic light scattering. Initial in vitro characterization confirmed that they were able to induce proliferation of human immune cells. This proliferative capability was enhanced when coupled with the natural lipid ligand of Pru p 3. The resultant formulation, called VLP-Complex, was also able to be transported by intestinal epithelial cells, without affecting the monolayer integrity. In light of all these results, VLP-Complex was furtherly tested in a mouse model of food allergy. Sublingual administration of VLP-Complex could effectively reduce some serological markers associated with allergic responses in mice, such as anti-Pru p 3 sIgE and sIgG2a. Noteworthy, no associated macroscopic, nephritic, or hepatic toxicity was detected, as assessed by weight, blood urea nitrogen (BUN) and galectin-3 analyses, respectively. Our results highlight the standardized production of allergen-coated TuMV-VLPs in N. benthamiana plants. The resulting formula exerts notable immunomodulatory properties without the need for potentially hazardous adjuvants. Accordingly, no detectable toxicity associated to their administration was detected. As a result, we propose them as good candidates to be furtherly studied in the treatment of immune-based pathologies.

show abstract

“…In this context, the patients' genetic background and their lifestyle, but also the environmental conditions in which the allergens are found and exposed [such as during an infection ( 55 ) or as accompanied by other epithelial stressors ( 27 )] are important variables that must be studied in detail to understand why sensitization ends up happening. LTPs are relevant in this line of study because they are naturally bound to lipidic molecules in the plant ( 14 ), thus conditioning that patients are typically co-exposed to both the protein and the lipid when getting in contact with the allergenic source. Hence, LTPs offer a good chance to understand how lipids can modulate the immunological state of the patient, working in conjunction with the allergen itself to induce the atopic phenotype in the organism.…”

Section: Discussionmentioning

confidence: 99%

“…LTPs constitute an important family of food and respiratory allergens. They are defined as small, basic, and thermostable proteins, with a highly conserved structure across the plant kingdom, characterized by a motif of eight residues of cysteine forming four disulfide bonds, and a cavity that allows them to harbor lipids ( 14 ). In total, 46 LTPs have been listed as allergens by the World Health Organization ( 15 ), being characterized by both their severity and high sensitization rates, especially in the Mediterranean region ( 16 ), but also in other countries, such as the UK ( 17 ).…”

Section: Ltps As Lipid Binding Proteinsmentioning

confidence: 99%

“…When different LTPs were purified from natural sources, the isolated ligand extracted from their cavities was always the CPT-PHS ligand, except for the case of wheat LTP1 (Tri a 14), for which 2 other different molecules where also found to be bound ( 12 ). The mechanism by which the CPT-PHS ligand enters inside the cavity of LTPs needs to be clarified but the actual hypothesis and studies related have been recently reviewed ( 14 ). This CPT-PHS ligand has been described to inhibit cell division in the plant and to avoid both pollination and the attack from herbivores ( 23 ).…”

Section: Allergenic Ltps Transport a Unique Kind Of Ligand When Studi...mentioning

confidence: 99%

See 1 more Smart Citation

Lipid Ligands and Allergenic LTPs: Redefining the Paradigm of the Protein-Centered Vision in Allergy

et al. 2022

Self Cite

View full text Add to dashboard Cite

Lipid Transfer Proteins (LTPs) have been described as one of the most prevalent and cross-reactive allergen families in the general population. They are widely distributed among the plant kingdom, as well as in different plant organs ranging from pollen to fruits. Thus, they can initiate allergic reactions with very different outcomes, such as asthma and food allergy. Several mouse models have been developed to unravel the mechanisms that lead LTPs to promote such strong sensitization patterns. Interestingly, the union of certain ligands can strengthen the allergenic capacity of LTPs, suggesting that not only is the protein relevant in the sensitization process, but also the ligands that LTPs carry in their cavity. In fact, different LTPs with pro-allergenic capacity have been shown to transport similar ligands, thus positioning lipids in a central role during the first stages of the allergic response. Here, we offer the latest advances in the use of experimental animals to study the topic, remarking differences among them and providing future researchers a tool to choose the most suitable model to achieve their goals. Also, recent results derived from metabolomic studies in humans are included, highlighting how allergic diseases alter the lipidic metabolism toward a pathogenic state in the individual. Altogether, this review offers a comprehensive body of work that sums up the background evidence supporting the role of lipids as modulators of allergic diseases. Studying the role of lipids during allergic sensitization might broaden our understanding of the molecular events leading to tolerance breakdown in the epithelium, thus helping us to understand how allergy is initiated and established in the individuals.

show abstract

Plant non-specific lipid transfer proteins: An overview

Cited by 58 publications

References 129 publications

Identification and molecular characterization of a novel non-specific lipid transfer protein (TdLTP2) from durum wheat

Identification and molecular characterization of a novel non-specific lipid transfer protein (TdLTP2) from durum wheat

Suitability of potyviral recombinant virus-like particles bearing a complete food allergen for immunotherapy vaccines

Lipid Ligands and Allergenic LTPs: Redefining the Paradigm of the Protein-Centered Vision in Allergy

Contact Info

Product

Resources

About