Lupin allergy: Uncovering structural features and epitopes of β-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes

Jose Jimenez-Lopez, E. Lima-Cabello, S. Melser, R.C. Foley, Karam Singh, D. Alché Juan

Research output: Chapter in Book/Conference paperConference paper

4 Citations (Scopus)

Abstract

© Springer International Publishing Switzerland 2015. The use of sweet lupins as a new food is resulting in an increasing number of cases of allergy reactions, particularly in atopic patients with other pre-existing legume allergies. We performed an extensive in silico analysis of seed β-conglutins, a new family of major allergen proteins in lupin, and a comparison to other relevant food allergens such as Ara h 1. We analyzed surface residues involved in conformational epitopes, lineal B- and T-cell epitopes variability, and changes in 2-D structural elements and 3D motives, with the aim to investigate IgE-mediated cross-reactivity among lupin, peanut, and other different legumes. Our results revealed that considerable structural differences exist, particularly affecting 2-D elements (loops and coils), and numerous micro-heterogeneities are present in fundamental residues directly involved in epitopes variability. Variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-reactivity among legumes.
Original languageEnglish
Title of host publicationBioinformatics and Biomedical Engineering
Subtitle of host publicationThird International Conference, IWBBIO 2015, Granada, Spain, April 15-17, 2015, Proceedings, Part I
EditorsFrancisco Ortuño, Ignacio Rojas
PublisherSpringer
Pages96-107
Volume1
ISBN (Electronic)9783319164830
ISBN (Print)9783319164823
DOIs
Publication statusPublished - 2015
Event3rd International Work-Conference on Bioinformatics and Biomedical Engineering - Granada, Spain
Duration: 15 Apr 201517 Apr 2015
Conference number: 3

Publication series

NameLecture Notes in Computer Science
PublisherSpringer
Volume9043
ISSN (Print)0302-9743
NameLecture Notes in Bioinformatics
PublisherSpringer
Volume9043

Conference

Conference3rd International Work-Conference on Bioinformatics and Biomedical Engineering
Abbreviated titleIWBBIO 2015
CountrySpain
CityGranada
Period15/04/1517/04/15

Fingerprint

Fabaceae
Epitopes
Hypersensitivity
Allergens
Immunoglobulin E
B-Lymphocyte Epitopes
Food
T-Lymphocyte Epitopes
Switzerland
Computer Simulation
Seeds
Lupinus angustifolius conglutin protein
Arachis
Proteins

Cite this

Jimenez-Lopez, J., Lima-Cabello, E., Melser, S., Foley, R. C., Singh, K., & Alché Juan, D. (2015). Lupin allergy: Uncovering structural features and epitopes of β-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes. In F. Ortuño, & I. Rojas (Eds.), Bioinformatics and Biomedical Engineering: Third International Conference, IWBBIO 2015, Granada, Spain, April 15-17, 2015, Proceedings, Part I (Vol. 1, pp. 96-107). (Lecture Notes in Computer Science ; Vol. 9043), (Lecture Notes in Bioinformatics; Vol. 9043). Springer. https://doi.org/10.1007/978-3-319-16483-0_10
Jimenez-Lopez, Jose ; Lima-Cabello, E. ; Melser, S. ; Foley, R.C. ; Singh, Karam ; Alché Juan, D. / Lupin allergy: Uncovering structural features and epitopes of β-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes. Bioinformatics and Biomedical Engineering: Third International Conference, IWBBIO 2015, Granada, Spain, April 15-17, 2015, Proceedings, Part I. editor / Francisco Ortuño ; Ignacio Rojas. Vol. 1 Springer, 2015. pp. 96-107 (Lecture Notes in Computer Science ). (Lecture Notes in Bioinformatics).
@inproceedings{ddf2dee123504bb2a5c7592370041be2,
title = "Lupin allergy: Uncovering structural features and epitopes of β-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes",
abstract = "{\circledC} Springer International Publishing Switzerland 2015. The use of sweet lupins as a new food is resulting in an increasing number of cases of allergy reactions, particularly in atopic patients with other pre-existing legume allergies. We performed an extensive in silico analysis of seed β-conglutins, a new family of major allergen proteins in lupin, and a comparison to other relevant food allergens such as Ara h 1. We analyzed surface residues involved in conformational epitopes, lineal B- and T-cell epitopes variability, and changes in 2-D structural elements and 3D motives, with the aim to investigate IgE-mediated cross-reactivity among lupin, peanut, and other different legumes. Our results revealed that considerable structural differences exist, particularly affecting 2-D elements (loops and coils), and numerous micro-heterogeneities are present in fundamental residues directly involved in epitopes variability. Variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-reactivity among legumes.",
author = "Jose Jimenez-Lopez and E. Lima-Cabello and S. Melser and R.C. Foley and Karam Singh and {Alch{\'e} Juan}, D.",
year = "2015",
doi = "10.1007/978-3-319-16483-0_10",
language = "English",
isbn = "9783319164823",
volume = "1",
series = "Lecture Notes in Computer Science",
publisher = "Springer",
pages = "96--107",
editor = "Francisco Ortu{\~n}o and Ignacio Rojas",
booktitle = "Bioinformatics and Biomedical Engineering",
address = "Netherlands",

}

Jimenez-Lopez, J, Lima-Cabello, E, Melser, S, Foley, RC, Singh, K & Alché Juan, D 2015, Lupin allergy: Uncovering structural features and epitopes of β-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes. in F Ortuño & I Rojas (eds), Bioinformatics and Biomedical Engineering: Third International Conference, IWBBIO 2015, Granada, Spain, April 15-17, 2015, Proceedings, Part I. vol. 1, Lecture Notes in Computer Science , vol. 9043, Lecture Notes in Bioinformatics, vol. 9043, Springer, pp. 96-107, 3rd International Work-Conference on Bioinformatics and Biomedical Engineering, Granada, Spain, 15/04/15. https://doi.org/10.1007/978-3-319-16483-0_10

Lupin allergy: Uncovering structural features and epitopes of β-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes. / Jimenez-Lopez, Jose; Lima-Cabello, E.; Melser, S.; Foley, R.C.; Singh, Karam; Alché Juan, D.

Bioinformatics and Biomedical Engineering: Third International Conference, IWBBIO 2015, Granada, Spain, April 15-17, 2015, Proceedings, Part I. ed. / Francisco Ortuño; Ignacio Rojas. Vol. 1 Springer, 2015. p. 96-107 (Lecture Notes in Computer Science ; Vol. 9043), (Lecture Notes in Bioinformatics; Vol. 9043).

Research output: Chapter in Book/Conference paperConference paper

TY - GEN

T1 - Lupin allergy: Uncovering structural features and epitopes of β-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes

AU - Jimenez-Lopez, Jose

AU - Lima-Cabello, E.

AU - Melser, S.

AU - Foley, R.C.

AU - Singh, Karam

AU - Alché Juan, D.

PY - 2015

Y1 - 2015

N2 - © Springer International Publishing Switzerland 2015. The use of sweet lupins as a new food is resulting in an increasing number of cases of allergy reactions, particularly in atopic patients with other pre-existing legume allergies. We performed an extensive in silico analysis of seed β-conglutins, a new family of major allergen proteins in lupin, and a comparison to other relevant food allergens such as Ara h 1. We analyzed surface residues involved in conformational epitopes, lineal B- and T-cell epitopes variability, and changes in 2-D structural elements and 3D motives, with the aim to investigate IgE-mediated cross-reactivity among lupin, peanut, and other different legumes. Our results revealed that considerable structural differences exist, particularly affecting 2-D elements (loops and coils), and numerous micro-heterogeneities are present in fundamental residues directly involved in epitopes variability. Variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-reactivity among legumes.

AB - © Springer International Publishing Switzerland 2015. The use of sweet lupins as a new food is resulting in an increasing number of cases of allergy reactions, particularly in atopic patients with other pre-existing legume allergies. We performed an extensive in silico analysis of seed β-conglutins, a new family of major allergen proteins in lupin, and a comparison to other relevant food allergens such as Ara h 1. We analyzed surface residues involved in conformational epitopes, lineal B- and T-cell epitopes variability, and changes in 2-D structural elements and 3D motives, with the aim to investigate IgE-mediated cross-reactivity among lupin, peanut, and other different legumes. Our results revealed that considerable structural differences exist, particularly affecting 2-D elements (loops and coils), and numerous micro-heterogeneities are present in fundamental residues directly involved in epitopes variability. Variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-reactivity among legumes.

U2 - 10.1007/978-3-319-16483-0_10

DO - 10.1007/978-3-319-16483-0_10

M3 - Conference paper

SN - 9783319164823

VL - 1

T3 - Lecture Notes in Computer Science

SP - 96

EP - 107

BT - Bioinformatics and Biomedical Engineering

A2 - Ortuño, Francisco

A2 - Rojas, Ignacio

PB - Springer

ER -

Jimenez-Lopez J, Lima-Cabello E, Melser S, Foley RC, Singh K, Alché Juan D. Lupin allergy: Uncovering structural features and epitopes of β-conglutin proteins in Lupinus Angustifolius L. with a focus on cross-allergenic reactivity to peanut and other legumes. In Ortuño F, Rojas I, editors, Bioinformatics and Biomedical Engineering: Third International Conference, IWBBIO 2015, Granada, Spain, April 15-17, 2015, Proceedings, Part I. Vol. 1. Springer. 2015. p. 96-107. (Lecture Notes in Computer Science ). (Lecture Notes in Bioinformatics). https://doi.org/10.1007/978-3-319-16483-0_10