Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS
Exposure to cow's milk constitutes one of the most common causes of food allergy. In addition, exposure to soy proteins has become relevant in a restricted proportion of milk allergic pediatric patients treated with soy formulae as a dairy substitute, because of the cross-allergenicity describe...
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2017
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_16159853_v17_n15-16_p_Candreva http://hdl.handle.net/20.500.12110/paper_16159853_v17_n15-16_p_Candreva |
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paper:paper_16159853_v17_n15-16_p_Candreva2023-06-08T16:25:24Z Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS Bos d 9.0101 Cow's milk Cross-reactivity Epitope mapping Gly m 5.0101 MALDI-TOF MS Soybean alpha casein beta casein epitope glycine kappa casein monoclonal antibody soybean protein allergen casein epitope milk protein peptide fragment soybean protein Article B lymphocyte child controlled study cross reaction epitope mapping human incubation time infant matrix assisted laser desorption ionization time of flight mass spectrometry milk milk allergy nonhuman priority journal protein motif reversed phase high performance liquid chromatography sequence analysis soybean taurine cattle amino acid sequence animal bovine chemistry epitope mapping female immunology matrix-assisted laser desorption-ionization mass spectrometry procedures soybean Allergens Amino Acid Sequence Animals Caseins Cattle Cross Reactions Epitope Mapping Epitopes, B-Lymphocyte Female Humans Infant Milk Milk Proteins Peptide Fragments Soybean Proteins Soybeans Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Exposure to cow's milk constitutes one of the most common causes of food allergy. In addition, exposure to soy proteins has become relevant in a restricted proportion of milk allergic pediatric patients treated with soy formulae as a dairy substitute, because of the cross-allergenicity described between soy and milk proteins. We have previously identified several cross-reactive allergens between milk and soy that may explain this intolerance. The purpose of the present work was to identify epitopes in the purified αS1-casein and the recombinant soy allergen Gly m 5.0101 (Gly m 5) using an α-casein-specific monoclonal antibody (1D5 mAb) through two different approaches for epitope mapping, to understand cross-reactivity between milk and soy. The 1D5 mAb was immobilized onto magnetic beads, incubated with the peptide mixture previously obtained by enzymatic digestion of the allergens, and the captured peptides were identified by MALDI-TOF MS analysis. On a second approach, the peptide mixture was resolved by RP-HPLC and immunodominant peptides were identified by dot blot with the mAb. Finally, recognized peptides were sequenced by MALDI-TOF MS. This novel MS based approach led us to identify and characterize four peptides on α-casein and three peptides on Gly m 5 with a common core motif. Information obtained from these cross-reactive epitopes allows us to gain valuable insight into the molecular mechanisms of cross-reactivity, to further develop new and more effective vaccines for food allergy. © 2017 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim 2017 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_16159853_v17_n15-16_p_Candreva http://hdl.handle.net/20.500.12110/paper_16159853_v17_n15-16_p_Candreva |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Bos d 9.0101 Cow's milk Cross-reactivity Epitope mapping Gly m 5.0101 MALDI-TOF MS Soybean alpha casein beta casein epitope glycine kappa casein monoclonal antibody soybean protein allergen casein epitope milk protein peptide fragment soybean protein Article B lymphocyte child controlled study cross reaction epitope mapping human incubation time infant matrix assisted laser desorption ionization time of flight mass spectrometry milk milk allergy nonhuman priority journal protein motif reversed phase high performance liquid chromatography sequence analysis soybean taurine cattle amino acid sequence animal bovine chemistry epitope mapping female immunology matrix-assisted laser desorption-ionization mass spectrometry procedures soybean Allergens Amino Acid Sequence Animals Caseins Cattle Cross Reactions Epitope Mapping Epitopes, B-Lymphocyte Female Humans Infant Milk Milk Proteins Peptide Fragments Soybean Proteins Soybeans Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| spellingShingle |
Bos d 9.0101 Cow's milk Cross-reactivity Epitope mapping Gly m 5.0101 MALDI-TOF MS Soybean alpha casein beta casein epitope glycine kappa casein monoclonal antibody soybean protein allergen casein epitope milk protein peptide fragment soybean protein Article B lymphocyte child controlled study cross reaction epitope mapping human incubation time infant matrix assisted laser desorption ionization time of flight mass spectrometry milk milk allergy nonhuman priority journal protein motif reversed phase high performance liquid chromatography sequence analysis soybean taurine cattle amino acid sequence animal bovine chemistry epitope mapping female immunology matrix-assisted laser desorption-ionization mass spectrometry procedures soybean Allergens Amino Acid Sequence Animals Caseins Cattle Cross Reactions Epitope Mapping Epitopes, B-Lymphocyte Female Humans Infant Milk Milk Proteins Peptide Fragments Soybean Proteins Soybeans Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS |
| topic_facet |
Bos d 9.0101 Cow's milk Cross-reactivity Epitope mapping Gly m 5.0101 MALDI-TOF MS Soybean alpha casein beta casein epitope glycine kappa casein monoclonal antibody soybean protein allergen casein epitope milk protein peptide fragment soybean protein Article B lymphocyte child controlled study cross reaction epitope mapping human incubation time infant matrix assisted laser desorption ionization time of flight mass spectrometry milk milk allergy nonhuman priority journal protein motif reversed phase high performance liquid chromatography sequence analysis soybean taurine cattle amino acid sequence animal bovine chemistry epitope mapping female immunology matrix-assisted laser desorption-ionization mass spectrometry procedures soybean Allergens Amino Acid Sequence Animals Caseins Cattle Cross Reactions Epitope Mapping Epitopes, B-Lymphocyte Female Humans Infant Milk Milk Proteins Peptide Fragments Soybean Proteins Soybeans Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| description |
Exposure to cow's milk constitutes one of the most common causes of food allergy. In addition, exposure to soy proteins has become relevant in a restricted proportion of milk allergic pediatric patients treated with soy formulae as a dairy substitute, because of the cross-allergenicity described between soy and milk proteins. We have previously identified several cross-reactive allergens between milk and soy that may explain this intolerance. The purpose of the present work was to identify epitopes in the purified αS1-casein and the recombinant soy allergen Gly m 5.0101 (Gly m 5) using an α-casein-specific monoclonal antibody (1D5 mAb) through two different approaches for epitope mapping, to understand cross-reactivity between milk and soy. The 1D5 mAb was immobilized onto magnetic beads, incubated with the peptide mixture previously obtained by enzymatic digestion of the allergens, and the captured peptides were identified by MALDI-TOF MS analysis. On a second approach, the peptide mixture was resolved by RP-HPLC and immunodominant peptides were identified by dot blot with the mAb. Finally, recognized peptides were sequenced by MALDI-TOF MS. This novel MS based approach led us to identify and characterize four peptides on α-casein and three peptides on Gly m 5 with a common core motif. Information obtained from these cross-reactive epitopes allows us to gain valuable insight into the molecular mechanisms of cross-reactivity, to further develop new and more effective vaccines for food allergy. © 2017 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim |
| title |
Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS |
| title_short |
Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS |
| title_full |
Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS |
| title_fullStr |
Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS |
| title_full_unstemmed |
Identification of cross-reactive B-cell epitopes between Bos d 9.0101(Bos Taurus) and Gly m 5.0101 (Glycine max) by epitope mapping MALDI-TOF MS |
| title_sort |
identification of cross-reactive b-cell epitopes between bos d 9.0101(bos taurus) and gly m 5.0101 (glycine max) by epitope mapping maldi-tof ms |
| publishDate |
2017 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_16159853_v17_n15-16_p_Candreva http://hdl.handle.net/20.500.12110/paper_16159853_v17_n15-16_p_Candreva |
| _version_ |
1768543295453003776 |