Antigenic and allergenic determinants of ovalbumin—III. MHC Ia-binding peptide (OA 323–339) interacts with human and rabbit specific antibodies

Johnsen, Geir; Elsayed, S.

doi:10.1016/0161-5890(90)90147-r

Cited by 47 publications

(34 citation statements)

References 31 publications

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“…Pep tide 323-339 was concluded to encompass one B cell epi tope [24], The present communication reports the antigenicity and allergenicity of the region 11-70 of the molecule. Five successive peptides were examined and assigned the reac tivities of this segment using rabbit antibodies and specific IgE from egg-allergic patients.…”

Section: Introductionmentioning

confidence: 78%

“…Earlier studies from our laboratory described the syn thesis of two OA epitopes 1-10and 323-339 [23,24]. In the present paper, five consecutively located peptides were synthesized and their activities were examined [39,40], Due to the ambiguity regarding epitope prediction in hy drophobic regions, the synthesis of a whole N-terminal segment was initiated at residue 11 and terminated at re sidue 70 [22,41,42],…”

Section: Discussionmentioning

confidence: 97%

“…The last solvent was continued for the same time, and then back to the initial composition (100% A:0% B). Aliquots of 100 pg peptide were originally run and the absorbance was monitored at 220 nm [24]. The initial concentration of the peptides (2 u.W) was usually used in 6-fold serial dilutions for examining their activity.…”

Section: The Synthesis and Purification O F The Peptidesmentioning

confidence: 99%

“…In previous studies the activities of two OA peptides (1-10 and 323-339) were studied [23,24], For 323-339, a correlation between peptide la interaction and MHC re striction were demonstrated and found responsible for 25-35% of BALBcT cell response to intact OA [25]. Pep tide 323-339 was concluded to encompass one B cell epi tope [24], The present communication reports the antigenicity and allergenicity of the region 11-70 of the molecule.…”

Section: Introductionmentioning

confidence: 99%

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Epitope Mapping of Region 11–70 of Ovalbumin (Gal d I) Using Five Synthetic Peptides

Elsayed

Stavseng²

1994

Int Arch Allergy Immunol

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Five successively located peptides, in region 11-70 of the major allergen of ovalbumin (OA) Gal d I (11–19, 20–33, 34–46, 47–55, 56–70), were obtained by manual solid-phase peptide synthesis. These peptides together with the previously reported OA region 1–10 comprise a segment of 70 amino acid residues located at the N-terminal of ovalbumin. The crude peptides were purified by gel filtration and reversed-phase high-performance liquid chromatographies and their sequences were verified. Polyclonal antibodies against the peptides conjugated to carrier protein (BSA) were raised in rabbits. Rocket line immunoelectrophoresis showed that four peptides (20–33, 34–46, 47–55 and 56–70), could deflect OA-line immunoprecipitates. The peptide’s affinity to rabbit polyclonal Ig was examined by quantitative precipitation inhibition and the results suggested that an epitope was encompassed in segments 34–55 and 4755. Allergenicity was tested by inhibition of specific IgE binding of ovalbumin, using several sera and a serum pool from 16 egg-allergic patients. The results showed that the allergenicity was distributed over the whole region. These findings suggested that: (a) the region 11–70 of OA seemed not to encompass continuous epitopes; (b) the antigenicity of this region was convincing for peptides 34–46 and 47–55; (c) the allergenicity, though dependent on the patient serum used, was distributed over the whole of region 11–70; (d) peptide 11–19, although weak antigenically was capable of specific IgE inhibition; (e) human and rabbit polyclonal antibodies did not show analogous affinities to the present peptides.

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Section: Introductionmentioning

confidence: 78%

Section: Discussionmentioning

confidence: 97%

Section: The Synthesis and Purification O F The Peptidesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Epitope Mapping of Region 11–70 of Ovalbumin (Gal d I) Using Five Synthetic Peptides

Elsayed

Stavseng²

1994

Int Arch Allergy Immunol

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“…For human consumption excessive heat-treatment of ovalbumin is relevant in view of the reported antigenic and allergenic properties of the native protein (Johnson and Elsayed, 1990;Kahlert et al, 1992), compared to heattreated forms (Ikura et al, 1992;Rumbo et al, 1996). Moreover, heat-treatment causes the protein to aggregate and allows the development of a gel structure (Weijers et al, 2004), a desired functionality for a food texturizer.…”

Section: Introductionmentioning

confidence: 99%

Deglycosylation of ovalbumin prohibits formation of a heat‐stable conformer

Groot

Kosters

Jongh

2007

Biotech & Bioengineering

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To study the influence of the carbohydrate-moiety of ovalbumin on the formation of the heat-stable conformer S-ovalbumin, ovalbumin is deglycosylated with PNGase-F under native conditions. Although the enzymatic deglycosylation procedure resulted in a complete loss of the ability to bind to Concavalin A column-material, only in about 50% the proteins lost their complete carbohydrate moiety, as demonstrated by mass spectrometry and size exclusion chromatography. Thermal stability and conformational changes were determined using circular dichroism and differential scanning calorimetry and demonstrated at ambient temperature no conformational changes due to the deglycosylation. Also the denaturation temperature of the processed proteins remained the same (77.4 +/- 0.4 degrees C). After heat treatment of the processed protein at 55 degrees C and pH 9.9 for 72 h, the condition that converts native ovalbumin into the heat-stable conformer (S-ovalbumin), only the material with the intact carbohydrate moiety forms this heat-stable conformer. The material that effectively lost its carbohydrate moiety appeared fully denatured and aggregated due to these processing conditions. These results indicate that the PNGase-F treatment of ovalbumin prohibits the formation and stabilization of the heat-stable conformer S-ovalbumin. Since S-ovalbumin in egg protein samples is known to affect functional properties, this work illustrates a potential route to control the quality of egg protein ingredients.

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Deciphering the interactions of phytochemicals with ovalbumin, the major food allergen from egg white: spectroscopic and computational studies

et al. 2022

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Ovalbumin (OVA), the major component of egg white, has been used as a model carrier protein to study the interaction of four bioactive phytochemicals 6-hydroxyflavone, chrysin, naringin, and naringenin. A static quenching mechanism was primarily associated with the complexation of the flavonoids with OVA. Hydrophobic forces play a major part in the stability of the complexes. The structural changes within the protein in response to flavonoid binding revealed a decrease in OVA's α-helical content. The hypothesized binding site for flavonoids in OVA overlaps with one or more immunoglobulin E-binding epitopes that may have some effect in the immunoglobulin E response pathway. The flavonoids remain in the same binding site throughout the simulation time and impart protein stability by forming different noncovalent interactions. This study presents comprehensive information about the interaction of the flavonoids with OVA and the associated structural variations after the binding, which might help researchers better comprehend similar medication pharmacodynamics and provide critical information for future therapeutic development.

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Antigenic and allergenic determinants of ovalbumin—III. MHC Ia-binding peptide (OA 323–339) interacts with human and rabbit specific antibodies

Cited by 47 publications

References 31 publications

Epitope Mapping of Region 11–70 of Ovalbumin (<i>Gal </i><i>d</i> I) Using Five Synthetic Peptides

Epitope Mapping of Region 11–70 of Ovalbumin (<i>Gal </i><i>d</i> I) Using Five Synthetic Peptides

Deglycosylation of ovalbumin prohibits formation of a heat‐stable conformer

Deciphering the interactions of phytochemicals with ovalbumin, the major food allergen from egg white: spectroscopic and computational studies

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