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3: Ion exchange chromatography of putative Pru p 3. (a) Represents the chromatogram while (b) represents the SDS-PAGE of the fractions corresponding to various peaks in the chromatogram.
Source publication
Lipid transfer proteins (LTPs) are a class of low molecular weight hydrophobic conserved proteins comprising four intramolecular disulphide bonds making the structure very resistant to proteolysis and harsh food processing conditions. These proteins are identified as strong allergens sensitizing through the gut and share epitopes with LTPs from clo...
Similar publications
Non-specific lipid transfer proteins (LTPs), present in multiple plant foods and pollens, are the predominant allergen in peach allergy in the Mediterranean region and may induce life-threatening allergic reactions. Although reasonably studied in adults, LTP allergy has been rarely described in children, and to the best of the author’s knowledge, n...
Tomato allergies have been extensively studied but component-resolved in vivo diagnosis with purified allergens has yet to be performed.
To evaluate the prevalence of sensitization to Sola l 3 in a Mediterranean population, and to compare the resulting sensitization profile with that of individuals sensitized to tomato, peach, and/or purified lipid...
Resistance of proteins to gastrointestinal digestion may play a role in determining immune-mediated adverse reactions to foods. However, digestion studies have largely been restricted to purified proteins and the impact of food processing and food matrices on protein digestibility is poorly understood.
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Background
Non-specific lipid-transfer protein (nsLTP) is a pan-allergen in the plant world, and a cause of significant concern as food allergen in the Mediterranean area, due to its general heat- and acid-resistance and hence the risk of severe allergic reactions. Pru p 3, the peach nsLTP, is considered the primary sensitizer to this allergen fami...
Background. The importance of issue is the rising incidence of allergies to volatile organic compounds, particularly in children and adults. This necessitates understanding the causes, risk factors, and methods for prevention and treatment. The purpose of the study was to clarify the relationship between the development of allergy to lipid transfer...
Citations
... And as observed by others a major tryptic cleavage site is found at Y79 which is responsible for generation of a Mr ~ 7 kDa fragment [15][16][17] . Previous studies showed pre-loading of Pru p 3 with linoleic acid enhanced Pru p 3 digestibility at pH 6.8 (duodenal conditions) even in the presence of bile salts 17 and competition binding studies indicated that bile salts were unable to displace the fluorescent lipid cis-parinaric acid 26 . It maybe the bile salts can bind to the unoccupied calyx and would account for the preferred chymotryptic cleavage site at Y79 which is more mobile and is made more accessible to chymotrypsin when a ligand is present in the lipid binding tunnel of Pru p 3 17 . ...
Sensitisation to the lipid transfer protein Pru p 3 is associated with severe allergic reactions to peach, the proteins stability being thought to play a role in its allergenicity. Lipid binding increases susceptibility of Pru p 3 to digestion and so the impact of bile salts on the in vitro gastrointestinal digestibility of Pru p 3 was investigated and digestion products mapped by SDS-PAGE and mass spectrometry. Bile salts enhanced the digestibility of Pru p 3 resulting in an ensemble of around 100 peptides spanning the protein’s sequence which were linked by disulphide bonds into structures of ~ 5–6 kDa. IgE binding studies with a serum panel from peach allergic subjects showed digestion reduced, but did not abolish, the IgE reactivity of Pru p 3. These data show the importance of including bile salts in vitro digestion systems and emphasise the need to profile of digestion in a manner that allows identification of immunologically relevant disulphide-linked peptide aggregates.
