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dc.contributorVall d'Hebron Barcelona Hospital Campus
dc.contributor.authorSkypala, Isabel J.
dc.contributor.authorAsero, Ricardo
dc.contributor.authorBarber, Domingo
dc.contributor.authorCecchi, Lorenzo
dc.contributor.authorDiaz Perales, Arazeli
dc.contributor.authorHoffmann‐Sommergruber, Karin
dc.contributor.authorLuengo Sanchez, Olga
dc.date.accessioned2022-01-13T12:27:42Z
dc.date.available2022-01-13T12:27:42Z
dc.date.issued2021-05
dc.identifier.citationSkypala IJ, Asero R, Barber D, Cecchi L, Diaz Perales A, Hoffmann-Sommergruber K, et al. Non-specific lipid-transfer proteins: Allergen structure and function, cross-reactivity, sensitization, and epidemiology. Clin Transl Allergy. 2021 May;11(3):1–13.
dc.identifier.issn2045-7022
dc.identifier.urihttp://hdl.handle.net/11351/6779
dc.descriptionAllergy; Epidemiology; Lipid transfer protein
dc.description.abstractBackground Discovered and described 40 years ago, non-specific lipid transfer proteins (nsLTP) are present in many plant species and play an important role protecting plants from stressors such as heat or drought. In the last 20 years, sensitization to nsLTP and consequent reactions to plant foods has become an increasing concern. Aim The aim of this paper is to review the evidence for the structure and function of nsLTP allergens, and cross-reactivity, sensitization, and epidemiology of nsLTP allergy. Materials and Methods A Task Force, supported by the European Academy of Allergy & Clinical Immunology (EAACI), reviewed current evidence and provide a signpost for future research. The search terms for this paper were “Non-specific Lipid Transfer Proteins”, “LTP syndrome”, “Pru p 3”, “plant food allergy”, “pollen-food syndrome”. Results Most nsLTP allergens have a highly conserved structure stabilised by 4-disulphide bridges. Studies on the peach nsLTP, Pru p 3, demonstrate that nsLTPs are very cross-reactive, with the four major IgE epitopes of Pru p 3 being shared by nsLTP from other botanically related fruits. These nsLTP allergens are to varying degrees resistant to heat and digestion, and sensitization may occur through the oral, inhaled or cutaneous routes. In some populations, Pru p 3 is the primary and sole sensitizing allergen, but many are poly-sensitised both to botanically un-related nsLTP in foods, and non-food sources of nsLTP such as Cannabis sativa, Platanus acerifolia, (plane tree), Ambrosia artemisiifolia (ragweed) and Artemisia vulgaris (mugwort). Initially, nsLTP sensitization appeared to be limited to Mediterranean countries, however more recent studies suggest clinically relevant sensitization occurs in North Atlantic regions and also countries in Northern Europe, with nsLTP sensitisation profiles being broadly similar. Discussion These robust allergens have the potential to sensitize and provoke symptoms to a large number of plant foods, including those which are raw, cooked or processed. It is unknown why some sensitized individuals develop clinical symptoms to foods whereas others do not, or indeed what other allergens besides Pru p 3 may be primary sensitising allergens. It is clear that these allergens are also relevant in non-Mediterranean populations and there needs to be more recognition of this. Conclusion Non-specific LTP allergens, present in a wide variety of plant foods and pollens, are structurally robust and so may be present in both raw and cooked foods. More studies are needed to understand routes of sensitization and the world-wide prevalence of clinical symptoms associated with sensitization to these complex allergens.
dc.language.isoeng
dc.publisherWiley
dc.relation.ispartofseriesClinical and Translational Allergy;11(3)
dc.rightsAttribution-NonCommercial 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/
dc.sourceScientia
dc.subjectAnafilaxi
dc.subjectAl·lèrgia alimentària - Diagnòstic
dc.subject.meshAllergens
dc.subject.meshFood Hypersensitivity
dc.subject.mesh/diagnosis
dc.titleNon-specific lipid-transfer proteins: Allergen structure and function, cross-reactivity, sensitization, and epidemiology
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1002/clt2.12010
dc.subject.decsalérgenos
dc.subject.decshipersensibilidad a los alimentos
dc.subject.decs/diagnóstico
dc.relation.publishversionhttps://doi.org/10.1002/clt2.12010
dc.type.versioninfo:eu-repo/semantics/publishedVersion
dc.audienceProfessionals
dc.contributor.organismesInstitut Català de la Salut
dc.contributor.authoraffiliation[Skypala IJ] Department of Allergy & Clinical Immunology, Royal Brompton & Harefield NHS Foundation Trust, Imperial College, London, UK. [Asero R] Ambulatorio di Allergologia, Clinica San Carlo, Milan, Italy. [Barber D] IMMA, School of Medicine, Universidad San Pablo CEU, CEU Universities, Madrid, Spain. RETIC ARADYAL RD16/0006/0015, Instituto de Salud Carlos III, Madrid, Spain. [Cecchi L] SOS Allergy and Clinical Immunology, USL Toscana Centro, Prato, Italy. [Diaz Perales A] Departamento de Biotecnología‐Biología Vegetal, Centro de Biotecnología y Genómica de Plantas (CBGP,UPM‐INIA),Universidad Politécnica de Madrid, Madrid, Spain. [Hoffmann-Sommergruber K] Department of Pathophysiology and Allergy Research, Medical University of Vienna, Austria. [Luengo O] Unitat d’Al·lèrgia, Servei de Medicina Interna, Vall d'Hebron Hospital Universitari, Barcelona, Spain. Universitat Autònoma de Barcelona, Bellaterra, Spain. ARADyAL, Barcelona, Spain
dc.identifier.pmid34025983
dc.identifier.wos000654371600001
dc.rights.accessrightsinfo:eu-repo/semantics/openAccess


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