Analysis of the IgE epitope profile of soybean allergen Gly m 4

Asthma epidemics have been shown to be related to where soybeans are loaded and handled, but data are scarce in the literature. This pilot study evaluated the levels of Gly m 1 in dust samples collected in Maringá, Brazil, a city with high soy production and processing. A dust impactor was used to collect seven isolated samples during 2015 and 2016. Samples were analyzed by an ELISA (enzyme-linked immunosorbent assay) detection method. Gly m 1 was found in all samples, ranging from 0.82–24.38 ng/m3 (median 2.41), regardless of the month or year evaluated. The levels of Gly m 1 were considered low, but the concentrations required to cause sensitization and symptoms are uncertain.

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IgE Epitope Profiling for Allergy Diagnosis and Therapy – Parallel Analysis of a Multitude of Potential Linear Epitopes Using a High Throughput Screening Platform

Frontiers in Immunology ◽

10.3389/fimmu.2020.565243 ◽

2020 ◽

Vol 11 ◽

Author(s):

Thorsten Krause ◽

Niels Röckendorf ◽

Barbara Meckelein ◽

Heike Sinnecker ◽

Christian Schwager ◽

...

Keyword(s):

High Throughput ◽

High Throughput Screening ◽

Parallel Analysis ◽

Allergy Diagnosis ◽

Diagnosis And Therapy ◽

Linear Epitopes ◽

Screening Platform ◽

Ige Epitope

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Fructooligosaccharide Inhibits the Absorption of β-conglycinin (A Major Soybean Allergen) in IPEC-J2

International Journal of Food Engineering ◽

10.1515/ijfe-2018-0116 ◽

2018 ◽

Vol 15 (1-2) ◽

Author(s):

Yuan Zhao ◽

Shiyao Zhang ◽

Xiaodong Zhang ◽

Li Pan ◽

Nan Bao ◽

...

Keyword(s):

Mass Spectrometry ◽

Enzymatic Hydrolysis ◽

Epithelial Cells ◽

Intestinal Epithelial Cells ◽

Time Dependent ◽

Dependent Manner ◽

Intestinal Epithelial ◽

Intracellular Accumulation ◽

Novel Therapeutic ◽

Soybean Allergen

AbstractDissecting the inhibited variation of allergen absorption could contribute to the development of novel therapeutic or preventive treatments for food/feed allergies. This study investigated the effects of fructooligosaccharide (FOS) on the absorption, intracellular accumulation of intact or hydrolysed β-conglycinin in porcine intestinal epithelial cells (IPEC-J2). As demonstrated by ELISA and immunoblotting, β-conglycinin was absorbed in a dose- and time-dependent manner (p < 0.05). Actually, β-conglycinin was easily transported and absorbed after enzymatic hydrolysis. Three peptides (52 kDa, 30 kDa and 25 kDa) were produced during transcellular absorption of intact or hydrolysed β-conglycinin. FOS inhibited the absorption of β-conglycinin, especially the 52 and 30 kDa peptides. The immunoreactive peptides derived from the 52, 35 or 22 kDa peptides were the substrings of the known epitopes determined by mass spectrometry and bioinformatic analyses. These results indicate that FOS can efficiently inhibit the absorption of 52 and 30 kDa peptides derived from β-conglycinin.

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