Effect of in vitro gastric and duodenal digestion on the allergenicity of grape lipid transfer protein.
ABSTRACT Severe grape allergy has been linked to lipid transfer protein (LTP) sensitization. LTPs are known to be resistant to pepsin digestion, although the effect of gastroduodenal digestion on its allergenicity has not been reported.
We sought to investigate the effect of gastric and gastroduodenal digestion on the allergenic activity of grape LTP.
The proteolytic stability of grape LTP was investigated by using an in vitro model of gastrointestinal digestion. The allergenicity of LTP and its digesta was assessed in vitro by means of IgE immunoblotting, RASTs, and in vivo skin prick tests in the same patients with grape allergy.
Grape LTP was resistant to gastric digestion, and yielded a 6000-d relative molecular mass C-terminally trimmed fragment after duodenal digestion. This fragment retained the in vitro IgE reactivity of the intact protein. Inclusion of phosphatidylcholine during gastric digestion protected the LTP to a limited extent against digestion. Digestion did not affect the in vivo (skin prick test) biologic activity of LTP.
The allergenic activity of grape LTP was highly resistant to in vitro digestion. This property might facilitate sensitization through the gastrointestinal tract and might also potentiate the ability of LTPs to elicit severe allergic reactions in sensitized individuals.
Purified natural allergens will facilitate the development of component-resolved diagnostic approaches, including allergen chips. This study contributes to our understanding of the role digestion plays in symptom elicitation in true food allergy.
- SourceAvailable from: Bernadett Berecz[Show abstract] [Hide abstract]
ABSTRACT: In order for a protein to elicit a systemic allergic response it must reach the circulatory system through the intestinal mucosa as a sufficiently large fragment with adequate structural integrity. Sunflower LTP and 2S albumins (SFA8 and three mixed fractions of Alb1 and Alb2) were digested in simulated gastric fluid (SGF) for 2h and the conditions were then changed to mimic the intestinal environment for a further 2h digestion. The effects of phosphatidylcholine (PC) and emulsification on the digestibility of the proteins were investigated. PC protected all of the proteins studied against both gastric and intestinal digestive enzymes but to different extents. Emulsification of SFA8 resulted in strong protection against digestion, which was further enhanced by the presence of PC in the SGF. These results highlight the importance of considering real food structures such as emulsified systems and also the gastrointestinal environment that proteins are exposed to once consumed when assessing allergenicity.Food Chemistry 06/2013; 138(4):2374-81. · 3.33 Impact Factor
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ABSTRACT: Nonspecific lipid transfer proteins (LTPs) are important allergens in fruits, vegetables, nuts, pollen, and latex. Despite their wide distribution throughout the plant kingdom, their clinical relevance is largely confined to the Mediterranean area. As they can sensitize via the gastrointestinal tract, LPTs are considered true food allergens, and IgE reactivity to LTPs is often associated with severe systemic symptoms. Although Pru p 3 represents the predominant LTP in terms of patients' IgE recognition, the contribution of pollen LTPs in primary sensitization cannot be ruled out. Due to structural homology, LTPs from different allergen sources are generally IgE cross-reactive. However, sensitization profiles among allergic patients are extremely heterogeneous, and individual cross-reactivity patterns can be restricted to a single LTP or encompass many different LTPs. Molecule-based approaches in allergy research and diagnosis are important for better understanding of LTP allergy and could assist clinicians with providing adequate patient-tailored advice.Current Allergy and Asthma Reports 09/2010; 10(5):326-35. · 2.75 Impact Factor
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ABSTRACT: Plant lipid transfer proteins (LTPs) are ubiquitous proteins that are found in divergent plant species. Although the exact function of LTPs is not fully understood, LTPs are conserved across a broad range of plant species. Because LTPs share structural features, there is an increased probability for significant allergic cross-reactivity. The molecular features of LTPs also decrease the probability of degradation due to cooking or digestion, thereby increasing the probability of systemic absorption and severe allergic reactions. LTP allergy, unlike other forms of anaphylaxis, tends to occur more frequently in areas of lower latitude. The geographic distribution of LTP allergy, along with evidence of increased sensitization after respiratory exposure, has led to the hypothesis that LTP-related food allergy may be secondary to sensitization via the respiratory route. Clinical reactions associated with LTPs have broad clinical phenotypes and can be severe in nature. Life-threatening clinical reactions have been associated with ingestion of a multitude of plant products. Component-resolved diagnosis has played a significant role in research applications for LTP allergy. In the future, component-resolved diagnosis may play a significant role in day-to-day clinical care. Also, quantitative analysis of LTPs in foodstuffs may allow for the identification and/or production of low-LTP foods, thereby decreasing the risk to patients with LTP allergy. Furthermore, sublingual immunotherapy may provide a therapeutic option for patients with LTP allergy.Clinical Reviews in Allergy & Immunology 11/2012; · 5.59 Impact Factor