Ligand binding to an allergenic lipid transfer protein enhances conformational flexibility resulting in an increase in susceptibility to gastroduodenal proteolysis

Abdullah, Syed Umer; Alexeev, Yuri; Johnson, Philip E.; Rigby, Neil M.; Mackie, Alan R.; Dhaliwal, Balvinder; Mills, E. N. Clare

doi:10.1038/srep30279

Title: Ligand binding to an allergenic lipid transfer protein enhances conformational flexibility resulting in an increase in susceptibility to gastroduodenal proteolysis

Journal Article · Tue Jul 26 00:00:00 EDT 2016 · Scientific Reports

DOI:https://doi.org/10.1038/srep30279· OSTI ID:1332942

Abdullah, Syed Umer ^[1]; Alexeev, Yuri ^[2]; Johnson, Philip E. ^[3]; Rigby, Neil M. ^[1]; Mackie, Alan R. ^[1]; Dhaliwal, Balvinder ^[4]; Mills, E. N. Clare ^[5]

Institute of Food Research, Conley (United Kingdom)
Institute of Food Research, Conley (United Kingdom); Argonne National Lab. (ANL), Argonne, IL (United States)
Institute of Food Research, Conley (United Kingdom); Univ. of Manchester, Manchester (United Kingdom); Univ. of Nebraska-Lincoln, Lincoln, NE (United States)
Univ. of Manchester, Manchester (United Kingdom)
Institute of Food Research, Conley (United Kingdom); Univ. of Manchester, Manchester (United Kingdom)

Non-specific lipid transfer proteins (LTPs) are a family of lipid-binding molecules that are widely distributed across flowering plant species, many of which have been identified as allergens. They are highly resistant to simulated gastroduodenal proteolysis, a property that may play a role in determining their allergenicity and it has been suggested that lipid binding may further increase stability to proteolysis. It is demonstrated that LTPs from wheat and peach bind a range of lipids in a variety of conditions, including those found in the gastroduodenal tract. Both LTPs are initially cleaved during gastroduodenal proteolysis at three major sites between residues 39–40, 56–57 and 79–80, with wheat LTP being more resistant to cleavage than its peach ortholog. The susceptibility of wheat LTP to proteolyic cleavage increases significantly upon lipid binding. This enhanced digestibility is likely to be due to the displacement of Tyr79 and surrounding residues from the internal hydrophobic cavity upon ligand binding to the solvent exposed exterior of the LTP, facilitating proteolysis. As a result, such knowledge contributes to our understanding as to how resistance to digestion can be used in allergenicity risk assessment of novel food proteins, including GMOs.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: Argonne National Laboratory - Argonne Leadership Computing Facility; USDOE

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1332942

Journal Information:: Scientific Reports, Vol. 6; ISSN 2045-2322

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 30 works

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