Structural Characterization of Act c 10.0101 and Pun g 1.0101—Allergens from the Non-Specific Lipid Transfer Protein Family
Autor: | Ivana Giangrieco, Maria Antonietta Ciardiello, Maksymilian Chruszcz, Andrea O’Malley, Lisa Tuppo, Anna Gawlicka-Chruszcz, S.S. Pote, Krzysztof Kowal |
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Rok vydání: | 2021 |
Předmět: |
Protein Conformation
alpha-Helical 0301 basic medicine cross-reactivity Actinidia Pharmaceutical Science Sequence (biology) nsLTP Crystallography X-Ray medicine.disease_cause Cross-reactivity Pomegranate Article Analytical Chemistry lcsh:QD241-441 03 medical and health sciences 0302 clinical medicine Allergen lcsh:Organic chemistry Non specific Drug Discovery medicine structure Physical and Theoretical Chemistry Prolamin Plant Proteins food allergy biology Chemistry Organic Chemistry SUPERFAMILY natural source Allergens Antigens Plant 030104 developmental biology 030228 respiratory system Biochemistry Chemistry (miscellaneous) Seeds Natural source biology.protein Molecular Medicine Carrier Proteins Plant lipid transfer proteins |
Zdroj: | Molecules, Vol 26, Iss 256, p 256 (2021) Molecules Volume 26 Issue 2 Molecules (Basel, Online) 26 (2021): 256. doi:10.3390/molecules26020256 info:cnr-pdr/source/autori:O'malley A.; Pote S.; Giangrieco I.; Tuppo L.; Gawlicka-Chruszcz A.; Kowal K.; Ciardiello M.A.; Chruszcz M./titolo:Structural characterization of act c 10.0101 and pun g 1.0101--allergens from the non-specific lipid transfer protein family/doi:10.3390%2Fmolecules26020256/rivista:Molecules (Basel, Online)/anno:2021/pagina_da:256/pagina_a:/intervallo_pagine:256/volume:26 |
ISSN: | 1420-3049 |
DOI: | 10.3390/molecules26020256 |
Popis: | 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 &alpha helical structures. The C-terminal sequence of Act c 10.0101 was updated based on our structural and mass spectrometry analysis. Information on proteins&rsquo 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. |
Databáze: | OpenAIRE |
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