Efficient expression of a soluble lipid transfer protein (LTP) ofPlatanus orientalisusing short peptide tags and structural comparison with the natural form

2015 ◽  
Vol 62 (2) ◽  
pp. 218-225 ◽  
Author(s):  
Farhad Salari ◽  
Fatemeh Vahedi ◽  
Jamshidkhan Chamani ◽  
Abdolreza Varasteh ◽  
Hanieh Ketabdar ◽  
...  
Keyword(s):  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Structural Comparison ◽  
Natural Form ◽  
Short Peptide ◽  
Transfer Protein ◽  
Peptide Tags ◽  
Efficient Expression

scholarly journals The key to the allergenicity of lipid transfer protein (LTP) ligands: A structural characterization

2021 ◽  
pp. 158928
Author(s):  
Zulema Gonzalez-Klein ◽  
Bruno Cuevas-Zuviria ◽  
Andrea Wangorsch ◽  
Guadalupe Hernandez-Ramirez ◽  
Diego Pazos-Castro ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein

scholarly journals Structural Characterization of Act c 10.0101 and Pun g 1.0101—Allergens from the Non-Specific Lipid Transfer Protein Family

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 256
Author(s):  
Andrea O’Malley ◽  
Swanandi Pote ◽  
Ivana Giangrieco ◽  
Lisa Tuppo ◽  
Anna Gawlicka-Chruszcz ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Lipid Transfer Protein ◽  
Mass Spectrometry Analysis ◽  
Lipid Transfer ◽  
Helical Structures ◽  
Spectrometry Analysis ◽  
X Ray Crystallography ◽  
Transfer Protein ◽  
Specific Lipid

(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.

Structural Stability and Surface Activity of Sunflower 2S Albumins and Nonspecific Lipid Transfer Protein

2010 ◽  
Vol 58 (10) ◽  
pp. 6490-6497 ◽  
Author(s):  
Bernadett Berecz ◽  
E. N. Clare Mills ◽  
László Tamás ◽  
Ferenc Láng ◽  
Peter R. Shewry ◽  
...  
Keyword(s):  
Structural Stability ◽  
Surface Activity ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
2S Albumins ◽  
Nonspecific Lipid Transfer Protein

scholarly journals cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family

2002 ◽  
Vol 32 (9) ◽  
pp. 1387-1387 ◽  
Author(s):  
A. Diaz-Perales ◽  
G. Garcia-Casado ◽  
R. Sanchez-Monge ◽  
F. J. Garcia-Selles ◽  
D. Barber ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Cdna Cloning ◽  
Lipid Transfer Protein ◽  
Protein Family ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Major Allergens
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