Document Detail


Pru p 3, the nonspecific lipid transfer protein from peach, dominates the immune response to its homolog in hazelnut.
MedLine Citation:
PMID:  21352239     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
To cite this article: Schulten V, Nagl B, Scala E, Bernardi ML, Mari A, Ciardiello MA, Lauer I, Scheurer S, Briza P, Jürets A, Ferreira F, Jahn-Schmid B, Fischer GF, Bohle B. Pru p 3, the nonspecific lipid transfer protein from peach, dominates the immune response to its homolog in hazelnut. Allergy 2011; DOI:10.1111/j.1398-9995.2011.02567.x. ABSTRACT: Background:  Nonspecific lipid transfer proteins (nsLTPs) are important food allergens. Often, patients allergic to the nsLTP in peach suffer from allergy to hazelnuts. We aimed to analyse the T-cell response to Cor a 8, the nsLTP in hazelnut and its immunological cross-reactivity with the nsLTP in peach, Pru p 3. Methods:  Cor a 8-reactive T-cell lines (TCL) established from patients allergic to hazelnut and peach were stimulated with 12-mer peptides representing the complete amino acid sequence of Cor a 8 to identify its T-cell-activating regions and with Pru p 3 to investigate cellular cross-reactivity. T-cell clones specific for different major T-cell-activating regions of Pru p 3 were stimulated with Cor a 8. Both nsLTPs were subjected to endolysosomal degradation assays. Immunoglobulin E (IgE) cross-reactivity between Cor a 8 and Pru p 3 was assessed in inhibition enzyme-linked immunosorbent assay. Results:  No major T-cell-activating region was found among 26 T-cell-reactive peptides identified in Cor a 8. Although generated with Cor a 8, 62% of the TCL responded more strongly to Pru p 3. This cross-reactivity was mediated by T cells specific for the immunodominant region Pru p 3(61-75) . Peptide clusters encompassing this region were generated during lysosomal degradation of both nsLTPs. Cor a 8 was more rapidly degraded by lysosomal proteases than Pru p 3. Pre-incubation of sera with Pru p 3 completely abolished IgE binding to Cor a 8, which was not the case vice versa. Conclusions:  T-cell reactivity to Cor a 8 is predominantly based on cross-reactivity with Pru p 3, indicating that the latter initiates sensitisation to its homolog in hazelnut. The limited allergenic potential of Cor a 8 seems to be associated with rapid lysosomal degradation during allergen processing and the lack of major T-cell-activating regions.
Authors:
V Schulten; B Nagl; E Scala; M L Bernardi; A Mari; M A Ciardiello; I Lauer; S Scheurer; P Briza; A Jürets; F Ferreira; B Jahn-Schmid; G F Fischer; B Bohle
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-2-26
Journal Detail:
Title:  Allergy     Volume:  -     ISSN:  1398-9995     ISO Abbreviation:  -     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-2-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7804028     Medline TA:  Allergy     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2011 John Wiley & Sons A/S.
Affiliation:
Department of Pathophysiology and Allergy Research, Medical University of Vienna, Vienna, Austria Christian Doppler Laboratory for Immunomodulation, Medical University of Vienna, Vienna, Austria Center for Clinical and Experimental Allergology, IDI-IRCCS, Rome Institute of Protein Biochemistry, CNR, Naples, Italy Division Allergology, Paul-Ehrlich-Institut, Langen, Germany Department of Molecular Biology, University of Salzburg, Salzburg, Austria Christian Doppler Laboratory for Allergy Diagnosis and Therapy, University of Salzburg, Salzburg, Austria Department of Blood Group Serology, Medical University of Vienna, Vienna, Austria.
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