http://www.cnr.it/ontology/cnr/individuo/prodotto/ID199817
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
- Pagina fine
- 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
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- ISI Web of Science (WOS) (literal)
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- 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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