Anno2013
AutoriBonura A, Corinti S, Schiavi E, Giacomazza D, Gianguzza F, Di Felice G, Colombo P
AbstractBackground: The major allergens in Parietaria pollen, Par j 1 and Par j 2, havebeen identified as lipid transfer proteins. The family of the Par j 1 allergens iscomposed of two isoforms, which differ by the presence of a 37 amino acid peptide(Par37) exclusive to the Par j 1.0101 isoform. The goal of this study was toelucidate the biological properties of the Par37 peptide.Methods: In silico analysis, spectrofluorimetric experiments and in vitro cell cultureassays were used to identify the biological properties of Par37. In addition, amouse model of sensitization was used to study the influence of Par37 in the murineimmune response.Results: In silico analysis predicted that Par37 displays characteristics of a hostdefence peptide. Spectrofluorimetric analysis, real-time PCR and ELISA assaysdemonstrated that Par37 possesses an LPS-binding activity influencing cell signallingin vitro. In RAW264.7 cells, LPS-induced IL-6 and TNF-a transcription andtranslation were inhibited after preincubation with Par37. Consistent with thesedata, inhibition of IFN-c secretion was observed in murine spleen cells and inhuman PBMC. Finally, mice immunized with the two Par j 1 isoforms differingin the presence or absence of the Par37 peptide showed different immunologicalbehaviours in vivo.Conclusions: This study demonstrates that the Par j 1.0101 allergen displays LPSbindingactivity due to the presence of a 37 amino acid COOH-terminal regionand that this region is capable of influencing cytokine and antibody responsesin vitro and in vivo.
RivistaAllergy
ISSN1398-9995
Impact factor
Volume68
Pagina inizio297
Pagina fine303
Autori IBFDaniela GIACOMAZZA
Linee di Ricerca IBFMD.P01.002.001
Sedi IBFIBF.PA