Isolation, expression and immunological characterization of a calcium-binding protein from Parietaria pollen

Bonura, Angela; Gulino, L; Trapani, Antonino; Felice, Gabriella Di; Tinghino, Raffaella; Amoroso, Saverio; Geraci, Domenico; Valenta, Rudolf; Westritschnig, Kerstin; Scala, Enrico; Mari, Adriano; Colombo, Piergiuseppe

doi:10.1016/j.molimm.2008.01.009

Cited by 11 publications

(9 citation statements)

References 33 publications

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“…Minor allergens are considered as markers of multiple pollen sensitization [15]. Profilins and calcium-binding proteins (polcalcins) are widespread even in botanically unrelated sources and, therefore, presumed to provoke a high potential of allergenic cross-reactivity [16,17]. This cross-reactivity is discussed to be a reason for nonresponse in allergen-specific immunotherapy (AIT).…”

Section: Discussionmentioning

confidence: 99%

Clinical Relevance of IgE to Profilin and/or Polcalcin in Pollen-Sensitized Patients

Nicoló

Braun

Eder

et al. 2016

Int Arch Allergy Immunol

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Background: Component-resolved diagnostics is gaining importance in allergy diagnostics. Allergen extracts contain components with different rates of prevalence and clinical relevance, which can be subdivided at molecular level into major and minor allergens. Clinical complaints are usually triggered by major allergens, while the role of sensitization to the panallergens profilin and polcalcin still remains unclear. Methods: Eighty-six patients from southern Bavaria with sensitization to the panallergens profilin (Bet v 2/Phl p 12) and/or polcalcin (Bet v 4/Phl p 7) were examined in regard to their sensitization to the 4 main botanic denominations Betulaceae, Oleaceae, Poaceae and Asteraceae by skin prick test and measurement of specific immunoglobulin E antibodies to natural allergen extracts as well as major allergen components rPhl p 1/5, rBet v 1, rOle e 1 and nArt v 1. Sensitization was rated as clinically relevant or irrelevant depending on anamnesis or intranasal allergen challenge. Results: Regarding the 4 botanic denominations, there was no significant difference in the incidence of sensitization to the panallergens profilin, polcalcin or both. The sensitization pattern does not alter when subdividing the cohort into clinically relevant and silent sensitization. We did not find clinically symptomatic sensitization to panallergens without cosensitization to a major allergen. Conclusions: Our results suggest that sole sensitization to panallergens seems to have no clinical relevance in allergic rhinoconjunctivitis. Clinical complaints seem to be triggered manly by major allergens. Thus, component-resolved allergy diagnostics is crucial in the diagnosis and treatment of polysensitized patients.

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Section: Discussionmentioning

confidence: 99%

Clinical Relevance of IgE to Profilin and/or Polcalcin in Pollen-Sensitized Patients

Nicoló

Braun

Eder

et al. 2016

Int Arch Allergy Immunol

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“…Parietaria spp represents a common cause of pollinosis in the Mediterranean area . Almost 30% of all the allergic subjects in southern Europe present a skin prick test (SPT) reactivity towards this pollen and more than 50% of these subjects have experienced bronchial asthma with high levels of bronchial hyperresponsiveness .…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Par j 1/Par j 2 mutant hybrid with reduced allergenicity for immunotherapy of Parietaria allergy

Bonura

Passantino

Costa

et al. 2012

Clin Experimental Allergy

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“…They belong to the family of lipid transfer proteins (LTP) which typically consist of four alpha-helices that are linked and stabilized by four disulphide bonds 14–17 . In addition to Par j 1 and Par j 2, highly cross-reactive allergens belonging to the family of profilins and calcium-binding allergens are minor allergens in Parietaria which are recognized typically by less than 10% of the patients 18,19 . The expression and purification of recombinant Par j 1 and Par j 2 resembling the fold of the corresponding wild-type allergens is difficult and requires eukaryotic hosts such as yeast expression systems capable of forming correct disulphide bonds 20 .…”

Section: Introductionmentioning

confidence: 99%

Expression and characterization of recombinant Par j 1 and Par j 2 resembling the allergenic epitopes of Parietaria judaica pollen

Dorofeeva

Colombo

Blanca

et al. 2019

Sci Rep

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The weed wall pellitory, Parietaria judaica, is one the most important pollen allergen sources in the Mediterranean area causing severe symptoms of hay fever and asthma in allergic patients. We report the expression of the major Parietaria allergens, Par j 1 and Par j 2 which belong to the family of lipid transfer proteins, in insect cells. According to circular dichroism analysis and gel filtration, the purified allergens represented folded and monomeric proteins. Insect cell-expressed, folded Par j 2 exhibited higher IgE binding capacity and more than 100-fold higher allergenic activity than unfolded Escherichia coli-expressed Par j 2 as demonstrated by IgE ELISA and basophil activation testing. IgE ELISA inhibition assays showed that Par j 1 and Par j 2, contain genuine and cross-reactive IgE epitopes. IgG antibodies induced by immunization with Par j 2 inhibited binding of allergic patients IgE to Par j 1 only partially. IgE inhibition experiments demonstrated that insect cell-expressed Par j 1 and Par j 2 together resembled the majority of allergenic epitopes of the Parietaria allergome and therefore both should be used for molecular diagnosis and the design of vaccines for allergen-specific immunotherapy of Parietaria allergy.

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Isolation, expression and immunological characterization of a calcium-binding protein from Parietaria pollen

Cited by 11 publications

References 33 publications

Clinical Relevance of IgE to Profilin and/or Polcalcin in Pollen-Sensitized Patients

Clinical Relevance of IgE to Profilin and/or Polcalcin in Pollen-Sensitized Patients

Characterization of a Par j 1/Par j 2 mutant hybrid with reduced allergenicity for immunotherapy of Parietaria allergy

Expression and characterization of recombinant Par j 1 and Par j 2 resembling the allergenic epitopes of Parietaria judaica pollen

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