Abstract
(1) Background: Non-specific lipid transfer proteins (nsLTPs), which belong to the prolamin superfamily, are potent allergens. While the biological role of LTPs is still not well understood, it is known that these proteins bind lipids. Allergen nsLTPs are characterized by significant stability and resistance to digestion. (2) Methods: nsLTPs from gold kiwifruit (Act c 10.0101) and pomegranate (Pun g 1.0101) were isolated from their natural sources and structurally characterized using X-ray crystallography (3) Results: Both proteins crystallized and their crystal structures were determined. The proteins have a very similar overall fold with characteristic compact, mainly α-helical structures. The C-terminal sequence of Act c 10.0101 was updated based on our structural and mass spectrometry analysis. Information on proteins’ sequences and structures was used to estimate the risk of cross-reactive reactions between Act c 10.0101 or Pun g 1.0101 and other allergens from this family of proteins. (4) Conclusions: Structural studies indicate a conformational flexibility of allergens from the nsLTP family and suggest that immunoglobulin E binding to some surface regions of these allergens may depend on ligand binding. Both Act c 10.0101 and Pun g 1.0101 are likely to be involved in cross-reactive reactions involving other proteins from the nsLTP family.
Highlights
Lipid transfer proteins (LTPs), called non-specific lipid transfer proteins, are known for their ability to bind and transport hydrophobic ligands [1,2,3,4]
Both protein chains include residues 1–92 that are folded into a compact, mainly α-helical structure that is characteristic for non-specific lipid transfer proteins (nsLTPs) (Figure 1)
The protein chains adopt very similar conformations and they superposed with Root Mean Square Deviation (RMSD) value of 0.3Å over 92 Cα
Summary
Lipid transfer proteins (LTPs), called non-specific lipid transfer proteins (nsLTPs), are known for their ability to bind and transport hydrophobic ligands [1,2,3,4]. The biological role of nsLTPs is still not well understood They transport these lipids between biological membranes primarily for defense, including structural adaptation, antimicrobial activity, and pathogenic resistance [5,6]. Plant nsLTPs are divided into two main subfamilies according to their molecular masses: 9-kDa and 7-kDa LTPs [10] Members of both the subfamilies are highly resistant to heat and denaturation [11,12]. We elucidated the crystal structures of Act c 10.0101 and Pun g 1.0101, nsLTP allergens from gold kiwifruit and pomegranate, respectively. These allergens both belong to the subfamily of 9-kDa LTPs. Structural studies highlight the conformational flexibility of both proteins and provide hints on their interactions with lipids. We have analyzed Act c 10.0101 and Pun g 1.0101 structures in connection to their potential to participate in cross-reactive allergic reactions
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