Pomegranate (Punica Granatum) Allergy: Clinical and Immunological Findings

Damiani, Elisabetta; Aloia, Anna Maria; Priore, M. G.; Nardulli, Stefania; Ferrannini, A.

doi:10.1016/s1081-1206(10)60176-7

Cited by 16 publications

(11 citation statements)

References 6 publications

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“…3 reacted with marked less intensity. Further protein bands were immunodetected at higher molecular masses but with less frequency and intensity; the 29-kDa band has been already reported [1,20]. Figure 3a shows that different proteins of approximately 8-14 kDa were separated by 2-D gel electrophoresis (2-DE).…”

Section: Resultsmentioning

confidence: 67%

Pomegranate (Punica granatum L.) Expresses Several nsLTP Isoforms Characterized by Different Immunoglobulin E-Binding Properties

Bolla

Zenoni

Scheurer

et al. 2014

Int Arch Allergy Immunol

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Background: Pomegranate allergy is associated with sensitization to non-specific lipid transfer proteins (nsLTPs). Our aim was to identify and characterize the non-specific nsLTPs expressed in pomegranate at the molecular level and to study their allergenic properties in terms of immunoglobulin E (IgE)-binding and cross-reactivity with peach nsLTP (Pru p 3). Methods: A non-equilibrium two-dimensional (2-D) electrophoretic approach based on acid-urea PAGE and sodium dodecyl sulfate PAGE was set up to separate pomegranate nsLTPs. Their immunoreactivity was tested by immunoblotting carried out with anti-Pru p 3 polyclonal antibodies and sera from pomegranate-allergic patients. For final identification, pomegranate nsLTPs were purified by chromatography and subjected to trypsin digestion and mass spectrometry (MS) analysis. For this purpose, the sequences obtained by cDNA cloning of three pomegranate nsLTPs were integrated in the database that was subsequently searched for MS data interpretation. Results: Four nsLTPs were identified by 2-D immunoblotting. The detected proteins showed different IgE-binding capacity and partial cross-reactivity with Pru p 3. cDNA cloning and MS analyses led to the identification of three nsLTP isoforms with 66-68% amino acid sequence identity named Pun g 1.0101, Pun g 1.0201 and Pun g 1.0301. Conclusions: By 2-D electrophoresis, we could separate different nsLTP isoforms possessing different IgE-binding properties, which might reflect peculiar allergenic potencies. The contribution of Pru p 3 to prime sensitization is not central as in other plant nsLTPs.

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Section: Resultsmentioning

confidence: 67%

Pomegranate (Punica granatum L.) Expresses Several nsLTP Isoforms Characterized by Different Immunoglobulin E-Binding Properties

Bolla

Zenoni

Scheurer

et al. 2014

Int Arch Allergy Immunol

View full text Add to dashboard Cite

show abstract

“…LTPs are now considered to be panallergens, causing severe systemic reactions to ingested fruits. The 29 kDa protein is the major protein in the crude extract, and was earlier reported as an allergic protein, but the protein was not isolated and characterised (Damiani et al, 2009;Gaig et al, 1999). In the present study, we report for the first time, a novel chitinase (PJC) from the juice of pomegranate.…”

Section: Discussionmentioning

confidence: 72%

“…Pomegranates have been infrequently reported to cause immediate hypersensitivity after ingestion (Damiani et al, 2009;Gaig et al, 1999). Moreover, there is no general consensus on which is the major pomegranate allergen.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, there is no general consensus on which is the major pomegranate allergen. Allergy to pomegranate was subsequently documented by means of a positive skin prick test (SPT) and in vitro assay results and, thereafter, 29-and 12-kDa protein allergens, that caused systemic reactions after fruit ingestion, were described (Damiani et al, 2009;Gaig et al, 1999). Earlier researchers have reported 9 and 12 kDa protein allergens from pomegranate juice as lipid transfer proteins (LTPs) (Zoccatelli et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…However, there have been relatively few investigations on the biochemical and structural characterisation of the proteins from pomegranate. Electrophoretic investigations on the crude extract of pomegranate juice indicated the presence of a 29 kDa protein as the major component (Damiani, Aloia, Priore, Nardulli, & Ferrannini, 2009;Gaig et al, 1999). We hereby report the purification and characterisation of this novel protein, possessing chitinase activity, from the juice of pomegranate.…”

Section: Introductionmentioning

confidence: 88%

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