Crystal structure of Pla l 1 reveals both structural similarity and allergenic divergence within the Ole e 1–like protein family

Stemeseder, Teresa; Freier, Regina; Wildner, Sabrina; Fuchs, Julian E.; Briza, Peter; Lang, Roland; Batanero, Eva; Lidholm, Jonas; Liedl, Klaus R.; Campo, Paloma; Hawranek, Thomas; Villalba, Mayte; Brandstetter, Hans; Ferreira, Fátima; Gadermaier, Gabriele

doi:10.1016/j.jaci.2016.10.035

Cited by 17 publications

(36 citation statements)

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“…The molecule exists as non-glycosylated and glycosylated variant, hence explaining the typical appearance as 2 bands. It has been recently demonstrated that the polypeptide backbone of Pla l 1 does not demonstrate IgE cross-reactivity with other allergens of the Ole e 1-like protein family [15,[17][18][19]. Consequently, IgE reactivity to the double band was inhibited with recombinant Pla l 1 but not with other pollen, even though they harbor allergenic (olive, ash, grass) as well as non-allergenic (birch) Ole e 1-like molecules.…”

Section: Discussionmentioning

confidence: 99%

“…Recombinant non-glycosyl-Int Arch Allergy Immunol 2018;177:97-106 DOI: 10.1159/000490004 ated Pla l 1 was expressed as soluble non-tagged protein in E. coli and purified using cation exchange and size exclusion chromatography as has been recently described [19].…”

Section: Pollen Extracts and Recombinant Pla Lmentioning

confidence: 99%

“…In a previous work investigating a Central European cohort, the allergen repertoire of English plantain was shown to be distinct from grasses and other pollen sources [8]. Pla l 1, the major allergen, has been extensively investigated and produced as recombinant protein in P. pastoris and Escherichia coli [15,[17][18][19]. The natural allergen is partially glycosylated and migrates as double band between 16 and 20 kDa in gel electrophoresis [15].…”

Section: Introductionmentioning

confidence: 99%

“…Pla l 1 is a member of the Ole e 1-like protein family sharing a short consensus sequence but only 28-40% overall sequence identity with other homologous allergens [19]. Relevant pollen allergens from this protein family are Ole e 1 (olive), Fra e 1 (ash), Phl p 11 (timothy grass), and Che a 1 (chenopod) [20,21].…”

Section: Introductionmentioning

confidence: 99%

“…Relevant pollen allergens from this protein family are Ole e 1 (olive), Fra e 1 (ash), Phl p 11 (timothy grass), and Che a 1 (chenopod) [20,21]. Recent studies showed a lack of IgE cross-reactivity of Pla l 1 with homologous allergens [19]. However, plantain pollen also harbors the panallergens profilin and polcalcin which are present in other pollen sources [8,[22][23][24][25][26][27][28][29][30][31].…”

Section: Introductionmentioning

confidence: 99%

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Do Plantago lanceolata Skin Prick Test-Positive Patients Display IgE to Genuine Plantain Pollen Allergens? Investigation of Pollen Allergic Patients from the North-East of France

Stemeseder¹,

Metz-Favre²,

Blay³

et al. 2018

Int Arch Allergy Immunol

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Background: English plantain (Plantago lanceolata) is an important weed pollen allergen source triggering allergic symptoms during summer. To elucidate genuine versus cross-reactive sensitization, we investigated IgE reactivity patterns and inhibition capacities of plantain-sensitized patients. Methods: Sera of 35 rhinoconjunctivitis patients from the north-east of France with positive skin prick tests (SPT) to Plantago lanceolata pollen were tested with clinically relevant allergen sources using ELISA, ImmunoCAP, and immunoblot inhibition. Results: The patients were multisensitized with additional reactivity to grass (94.3%), ash (74.3%), birch (71.4%), and mugwort (55.2%) pollen in SPT. Sensitization prevalence to allergen molecules was 34.3% (Pla l 1), 94.3% (Phl p 1/5), 60.0% (Ole e 1), 65.7% (Bet v 1), 37.1% (profilin), and 40.0% (CCD). In immunoblot, IgE reactivity to plantain pollen was inhibited with relevant pollen extracts and purified rPla l 1. Two sera did not reveal any IgE cross-reactivity, while reactivity to plantain was efficiently inhibited by grass pollen in the sera of 10 patients. The sera from 17 different patients could be inhibited by grass, birch, or ash pollen to varying degrees. Thus, only 37.1% of our patients demonstrated true plantain pollen sensitization, while 62.9% were solely positive due to IgE cross-reactive molecules from other clinically relevant pollen. Conclusions: Plantain pollen-sensitized patients are multi-reactors demonstrating varying and complex IgE-reactivity profiles. In vivo and in vitro tests using extracts are typically blurred due to the presence of homologous allergens or CCD in grass, birch, or ash pollen. So far, Pla l 1 represents the only indicative marker allergen for the diagnosis of genuine plantain pollen sensitization.

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Section: Discussionmentioning

confidence: 99%

Section: Pollen Extracts and Recombinant Pla Lmentioning

confidence: 99%