Relationship between IgE Levels Specific for Ragweed Pollen Extract, Amb a 1 and Cross-Reactive Allergen Molecules

Zbîrcea, Lauriana‐Eunice; Buzan, Maria‐Roxana; Grijincu, Manuela; Babaev, Elijahu; Stolz, Frank; Valenta, Rudolf; Păunescu, Virgil; Panaitescu, Carmen; Chen, Kuan-Wei

doi:10.3390/ijms24044040

Cited by 7 publications

(5 citation statements)

References 44 publications

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“…For example, it was found that profilin can be a primary airborne sensitizer ( 48 ). According to frequencies of IgE recognition, profilin is an important allergen in ragweed pollen allergy ( 49 ) and in mugwort pollen allergy ( 18 ). For several other allergen sources, profilins were reported to be major allergens such as for eggplant ( 50 ), Amaranthus ( 51 ), melon ( 52 – 54 ), orange ( 55 ), and oilseed rape ( 56 ).…”

Section: Discussionmentioning

confidence: 99%

The cytoskeletal protein profilin is an important allergen in saltwort (Salsola kali)

Peterkova,

Trifonova,

Gattinger

et al. 2024

Front. Immunol.

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Pollen from Salsola kali, i.e., saltwort, Russian thistle, is a major allergen source in the coastal regions of southern Europe, in Turkey, Central Asia, and Iran. S. kali-allergic patients mainly suffer from hay-fever (i.e., rhinitis and conjunctivitis), asthma, and allergic skin symptoms. The aim of this study was to investigate the importance of individual S. kali allergen molecules. Sal k 1, Sal k 2, Sal k 3, Sal k 4, Sal k 5, and Sal k 6 were expressed in Escherichia coli as recombinant proteins containing a C-terminal hexahistidine tag and purified by nickel affinity chromatography. The purity of the recombinant allergens was analyzed by SDS-PAGE. Their molecular weight was determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, and their fold and secondary structure were studied by circular dichroism (CD) spectroscopy. Sera from clinically well-characterized S. kali-allergic patients were used for IgE reactivity and basophil activation experiments. S. kali allergen-specific IgE levels and IgE levels specific for the highly IgE cross-reactive profilin and the calcium-binding allergen from timothy grass pollen, Phl p 12 and Phl p 7, respectively, were measured by ImmunoCAP. The allergenic activity of natural S. kali pollen allergens was studied in basophil activation experiments. Recombinant S. kali allergens were folded when studied by CD analysis. The sum of recombinant allergen-specific IgE levels and allergen-extract-specific IgE levels was highly correlated. Sal k 1 and profilin, reactive with IgE from 64% and 49% of patients, respectively, were the most important allergens, whereas the other S. kali allergens were less frequently recognized. Specific IgE levels were highest for profilin. Of note, 37% of patients who were negative for Sal k 1 showed IgE reactivity to Phl p 12, emphasizing the importance of the ubiquitous cytoskeletal actin-binding protein, profilin, for the diagnosis of IgE sensitization in S. kali-allergic patients. rPhl p 12 and rSal k 4 showed equivalent IgE reactivity, and the clinical importance of profilin was underlined by the fact that profilin-monosensitized patients suffered from symptoms of respiratory allergy to saltwort. Accordingly, profilin should be included in the panel of allergen molecules for diagnosis and in molecular allergy vaccines for the treatment and prevention of S. kali allergy.

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Section: Discussionmentioning

confidence: 99%

The cytoskeletal protein profilin is an important allergen in saltwort (Salsola kali)

Peterkova,

Trifonova,

Gattinger

et al. 2024

Front. Immunol.

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“…IgE binding in ImmunoCAP was performed by using commercially available Amb a 1 (w230) and ragweed pollen extract (w1) ImmunoCAPs, whereas rAmb a 6 was first bound to Streptavidin ImmunoCAP (o212, Thermo Fisher Scientific/Phadia, Uppsala, Sweden) as described in [ 19 ]. Specific IgE levels were measured on the Phadia 100 and Phadia 250 platform (Thermo Fisher Scientific).…”

Section: Methodsmentioning

confidence: 99%

“…Patients sensitized to ragweed pollen were found to have complex IgE sensitization patterns [ 18 ]. Patients tended to report more symptoms when sensitized to pan-allergens in addition to Amb a 1 [ 18 , 19 ]. Importantly, the allergenic activity of the individual ragweed allergens needs to be evaluated in more detail because the frequency of IgE recognition does not take into consideration this important parameter for the clinical relevance of a given allergen [ 20 , 21 , 22 ].…”

Section: Introductionmentioning

confidence: 99%

Non-Specific Lipid Transfer Protein Amb a 6 Is a Source-Specific Important Allergenic Molecule in Ragweed Pollen

Grijincu,

Tănasie,

Zbîrcea

et al. 2024

IJMS

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Pollen from common ragweed is an important allergen source worldwide and especially in western and southern Romania. More than 100 million patients suffer from symptoms of respiratory allergy (e.g., rhinitis, asthma) to ragweed pollen. Among the eleven characterized allergens, Amb a 6 is a non-specific lipid transfer protein (nsLTP). nsLTPs are structurally stable proteins in pollen and food from different unrelated plants capable of inducing severe reactions. The goal of this study was to produce Amb a 6 as a recombinant and structurally folded protein (rAmb a 6) and to characterize its physicochemical and immunological features. rAmb a 6 was expressed in Spodoptera frugiperda Sf9 cells as a secreted protein and characterized by mass spectrometry and circular dichroism (CD) spectroscopy regarding molecular mass and fold, respectively. The IgE-binding frequency towards the purified protein was evaluated using sera from 150 clinically well-characterized ragweed-allergic patients. The allergenic activities of rAmb a 6 and the nsLTP from the weed Parietaria judaica (Par j 2) were evaluated in basophil activation assays. rAmb a 6-specific IgE reactivity was associated with clinical features. Pure rAmb a 6 was obtained by insect cell expression. Its deduced molecular weight corresponded to that determined by mass spectrometry (i.e., 10,963 Da). rAmb a 6 formed oligomers as determined by SDS-PAGE under non-reducing conditions. According to multiple sequence comparisons, Amb a 6 was a distinct nsLTP with less than 40% sequence identity to currently known plant nsLTP allergens, except for nsLTP from Helianthus (i.e., 52%). rAmb a 6 is an important ragweed allergen recognized by 30% of ragweed pollen allergic patients. For certain patients, rAmb a 6-specific IgE levels were higher than those specific for the major ragweed allergen Amb a 1 and analysis also showed a higher allergenic activity in the basophil activation test. rAmb a 6-positive patients suffered mainly from respiratory symptoms. The assumption that Amb a 6 is a source-specific ragweed allergen is supported by the finding that none of the patients showing rAmb a 6-induced basophil activation reacted with Par j 2 and only one rAmb a 6-sensitized patient had a history of plant food allergy. Immunization of rabbits with rAmb a 6 induced IgG antibodies which strongly inhibited IgE binding to rAmb a 6. Our results demonstrate that Amb a 6 is an important source-specific ragweed pollen allergen that should be considered for diagnosis and allergen-specific immunotherapy of ragweed pollen allergy.

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“…Rat basophil leukemia (huRBL) RS-ATL8 cells, transfected to express the human high-affinity IgE receptor on their surface [ 29 ], were cultivated and plated, as previously described [ 30 ]. The cells were loaded with 1:10-diluted patient serum from five ragweed-allergic patients, two sensitized to rAmb a 9 (OD ≥ 0.4) and four patients sensitized to rAmb a 10 (OD ≥ 0.4), and incubated overnight at 37 °C, 5% CO 2 .…”

Section: Methodsmentioning

confidence: 99%

Cross-Reactivity of Ragweed Pollen Calcium-Binding Proteins and IgE Sensitization in a Ragweed-Allergic Population from Western Romania

Zbîrcea,

Buzan,

Grijincu

et al. 2024

ARM

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Ragweed pollen allergy is the most common seasonal allergy in western Romania. Prolonged exposure to ragweed pollen may induce sensitization to pan-allergens such as calcium-binding proteins (polcalcins) and progression to more severe symptoms. We aimed to detect IgE sensitization to recombinant Amb a 9 and Amb a 10 in a Romanian population, to assess their potential clinical relevance and cross-reactivity, as well as to investigate the relation with clinical symptoms. rAmb a 9 and rAmb a 10 produced in Escherichia coli were used to detect specific IgE in sera from 87 clinically characterized ragweed-allergic patients in ELISA, for basophil activation experiments and rabbit immunization. Rabbit rAmb a 9- and rAmb a 10-specific sera were used to detect possible cross-reactivity with rArt v 5 and reactivity towards ragweed and mugwort pollen extracts. The results showed an IgE reactivity of 25% to rAmb a 9 and 35% to rAmb a 10. rAmb a 10 induced basophil degranulation in three out of four patients tested. Moreover, polcalcin-negative patients reported significantly more skin symptoms, whereas polcalcin-positive patients tended to report more respiratory symptoms. Furthermore, both rabbit antisera showed low reactivity towards extracts and showed high reactivity to rArt v 5, suggesting strong cross-reactivity. Our study indicated that recombinant ragweed polcalcins might be considered for molecular diagnosis.

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Relationship between IgE Levels Specific for Ragweed Pollen Extract, Amb a 1 and Cross-Reactive Allergen Molecules

Cited by 7 publications

References 44 publications

The cytoskeletal protein profilin is an important allergen in saltwort (Salsola kali)

The cytoskeletal protein profilin is an important allergen in saltwort (Salsola kali)

Non-Specific Lipid Transfer Protein Amb a 6 Is a Source-Specific Important Allergenic Molecule in Ragweed Pollen

Cross-Reactivity of Ragweed Pollen Calcium-Binding Proteins and IgE Sensitization in a Ragweed-Allergic Population from Western Romania

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