Effects of Maillard reaction on structural modification and potential allergenicity of peanut 7S globulin (Ara h 1)

2020 ◽  
Vol 100 (15) ◽  
pp. 5617-5626
Author(s):  
Yunfeng Shi ◽  
Minjia Wang ◽  
Yanting Ding ◽  
Jiahui Chen ◽  
Bing Niu ◽  
...  
2012 ◽  
Vol 129 (2) ◽  
pp. AB177
Author(s):  
C.P. Mattison ◽  
C.C. Grimm ◽  
W.A. Desormeaux ◽  
S. Ruan ◽  
S.J. Maleki

2013 ◽  
Vol 116 (2) ◽  
pp. 424-434 ◽  
Author(s):  
M. Teodorowicz ◽  
D. Świątecka ◽  
H. Savelkoul ◽  
H. Wichers ◽  
E. Kostyra

Allergies ◽  
2021 ◽  
Vol 1 (1) ◽  
pp. 63-91
Author(s):  
Annick Barre ◽  
Christophe Nguyen ◽  
Claude Granier ◽  
Hervé Benoist ◽  
Pierre Rougé

Sequential IgE-binding epitopes were identified on the molecular surface of the Pis v 1 (2S albumin), Pis v 2 (11S globulin/legumin) and Pis v 3 (7S globulin/vicilin)—major allergens from pistachio (Pistacia vera) seeds—using the Spot technique. They essentially consist of hydrophilic and electropositively charged residues well exposed on the surface of the allergens. Most of the epitopic regions identified on Pis v 1 and Pis v 3 do not coincide with the putative N-glycosylation sites and thus are not considered as glycotopes. Surface analysis of these epitopic regions indicates a high degree of conformational similarity with the previously identified epitopic regions of the corresponding allergens Ana o 1 (vicilin), Ana o 2 (legumin) and Ana o 3 (2S albumin) from the cashew (Anacardium occidentale) nut. These results offer a molecular basis for the IgE-binding cross-reactivity often observed between pistachio and cashew nut. They support the recommendation for prescribing pistachio avoidance in cashew allergic patients. Other conformational similarities were identified with the corresponding allergens Ses i 1 (2S albumin), Ses i 3 (vicilin) and Ses i 6 (legumin) from sesame (Sesamum indicum), and Jug r 1 (2S albumin), Jug r 2 (vicilin) and Jug r 4 (legumin) from walnut (Juglans regia). Conversely, conformation of most of the epitopic regions of the pistachio allergens often differs from that of epitopes occurring on the molecular surface of the corresponding Ara h 1 (vicilin), Ara h 2 (2S albumin) and Ara h 3 (legumin) allergens from peanut (Arachis hypogaea).


Author(s):  
Pham V. Huong ◽  
Stéphanie Bouchet ◽  
Jean-Claude Launay

Microstructure of epitaxial layers of doped GaAs and its crystal growth dynamics on single crystal GaAs substrate were studied by Raman microspectroscopy with a Dilor OMARS instrument equipped with a 1024 photodiode multichannel detector and a ion-argon laser Spectra-Physics emitting at 514.5 nm.The spatial resolution of this technique, less than 1 μm2, allows the recording of Raman spectra at several spots in function of thickness, from the substrate to the outer deposit, including areas around the interface (Fig.l).The high anisotropy of the LO and TO Raman bands is indicative of the orientation of the epitaxial layer as well as of the structural modification in the deposit and in the substrate at the interface.With Sn doped, the epitaxial layer also presents plasmon in Raman scattering. This fact is already very well known, but we additionally observed that its frequency increases with the thickness of the deposit. For a sample with electron density 1020 cm-3, the plasmon L+ appears at 930 and 790 cm-1 near the outer surface.


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