The major allergen of the Parietaria pollen contains an LPS-binding region with immuno-modulatory activity (Articolo in rivista)

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Label
  • The major allergen of the Parietaria pollen contains an LPS-binding region with immuno-modulatory activity (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1111/all.12086 (literal)
Alternative label
  • Bonura A, Corinti S, Schiavi E, Giacomazza D, Gianguzza F, Di Felice G, Colombo P (2013)
    The major allergen of the Parietaria pollen contains an LPS-binding region with immuno-modulatory activity
    in Allergy (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Bonura A, Corinti S, Schiavi E, Giacomazza D, Gianguzza F, Di Felice G, Colombo P (literal)
Pagina inizio
  • 297 (literal)
Pagina fine
  • 303 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://onlinelibrary.wiley.com/doi/10.1111/all.12086/abstract;jsessionid=8055C5EBA025C19B41B83DD05D657640.f02t03 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 68 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 3 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biomedicina ed Immunologia Molecolare \"Alberto Monroy\" del Consiglio Nazionale delle Ricerche, Palermo; Dipartimento di Malattie Infettive, Parassitarie e Immuno-mediate, Istituto Superiore di Sanità, Roma; Istituto di Biofisica del Consiglio Nazionale delle Ricerche (UOS Palermo), Palermo; Dipartimento di Scienze e Tecnologie Molecolari e Biomolecolari, Università degli Studi di Palermo, Palermo, Italy (literal)
Titolo
  • The major allergen of the Parietaria pollen contains an LPS-binding region with immuno-modulatory activity (literal)
Abstract
  • Background: The major allergens in Parietaria pollen, Par j 1 and Par j 2, have been identified as lipid transfer proteins. The family of the Par j 1 allergens is composed 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 to elucidate the biological properties of the Par37 peptide. Methods: In silico analysis, spectrofluorimetric experiments and in vitro cell culture assays were used to identify the biological properties of Par37. In addition, a mouse model of sensitization was used to study the influence of Par37 in the murine immune response. Results: In silico analysis predicted that Par37 displays characteristics of a host defence peptide. Spectrofluorimetric analysis, real-time PCR and ELISA assays demonstrated that Par37 possesses an LPS-binding activity influencing cell signalling in vitro. In RAW264.7 cells, LPS-induced IL-6 and TNF-a transcription and translation were inhibited after preincubation with Par37. Consistent with these data, inhibition of IFN-c secretion was observed in murine spleen cells and in human PBMC. Finally, mice immunized with the two Par j 1 isoforms differing in the presence or absence of the Par37 peptide showed different immunological behaviours in vivo. Conclusions: This study demonstrates that the Par j 1.0101 allergen displays LPSbinding activity due to the presence of a 37 amino acid COOH-terminal region and that this region is capable of influencing cytokine and antibody responses in vitro and in vivo. (literal)
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