The key to the allergenicity of lipid transfer protein (LTP) ligands: A structural characterization

Plant lipid transfer proteins are a large family that can be found in all land plants. They have hydrophobic cavity allows them to harbor lipids and facilitates their traffic between membranes. However, humans, this plant protein is responsible for the main food allergies Mediterranean area. Nevertheless, not only itself but also its ligand relevant allergic sensitization. The aim of present work analyse natural ligands carried by four allergenic LTPs (Tri 14, Art v 3, Par j 2, Ole e 7), compared with previously identified Pru p 3 (CPT-PHS ligand), clarify role within immunological reactions. Results showed studied shared chemical identity, which presence polar head was essential protein-ligand binding. This transported through skin cellular model, phosphorylated phytosphingosine could detected as result cell metabolism. Since sphingosine kinase 1 overexpressed keratinocytes incubated LTP-ligand complex, enzyme might phosphorylation fraction CPT-PHS ligand. way, phytosphingosine-1-phosphate mimicking human inflammatory mediator sphingosine-1-phosphate, explaining why associated more severe responses. In conclusion, contributes understanding nature behavior allergens, would help gain insight into during