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Glycosylation enhances allergenic activity of major bee venom allergen Api m 1 by adding IgE epitopes

Gattinger, Pia, Bidovec-Stojkovic, Urska, Zidarn, Mihaela, Korosec, Peter, Valenta, Rudolf, Mittermann, Irene·2021·Journal of Allergy and Clinical Immunology
DOI 10.1016/j.jaci.2020.10.002
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FIG 1 Circular dichroism analysis of nApi m 1 and rApi m 1. A, Scans showing molar ellipticity (y-axes) at given wavelengths (x-axes) are presented for nApi m 1 (Api m 1 nat [ left ]) and rApi m 1 (Api m 1 rec [ right ]). (B) Phospholipase A2 activity of nApi m 1 and rApi m 1. Results are expressed as time-dependent increases in absorbance (mOD405nm/min). Mean values of duplicate measurements are shown.
FIG 1 Circular dichroism analysis of nApi m 1 and rApi m 1. A, Scans showing molar ellipticity (y-axes) at given wavelengths (x-axes) are presented for nApi m 1 (Api m 1 nat [ left ]) and rApi m 1 (Api m 1 rec [ right ]). (B) Phospholipase A2 activity of nApi m 1 and rApi m 1. Results are expressed as time-dependent increases in absorbance (mOD405nm/min). Mean values of duplicate measurements are shown.CC-BY · From the PDF
FIG 2 Allergenic activity of nApi m 1 and rApi m 1. Rat basophil leukemia cells were loaded with serum IgE from patients with bee venom allergy (Table E1 [patients 3, 4, 6, 9, and 12]) and incubated with different concentrations of nApi m 1 or rApi m 1 (100, 10, 1, 0.1, and 0.01 ng/mL) (x-axes) or buffer alone. b -hexosaminidase releases are displayed as mean percentages of duplicate determinations displaying the ranges of variance of total b -hexosaminidase release minus buffer on the y-axes.
FIG 2 Allergenic activity of nApi m 1 and rApi m 1. Rat basophil leukemia cells were loaded with serum IgE from patients with bee venom allergy (Table E1 [patients 3, 4, 6, 9, and 12]) and incubated with different concentrations of nApi m 1 or rApi m 1 (100, 10, 1, 0.1, and 0.01 ng/mL) (x-axes) or buffer alone. b -hexosaminidase releases are displayed as mean percentages of duplicate determinations displaying the ranges of variance of total b -hexosaminidase release minus buffer on the y-axes.CC-BY · From the PDF
FIG E1. A, Coomassie blue-stained SDS-PAGE showing nApi m 1 and rApi m 1. Nitrocellulose-blotted nApi m 1 and rApi m 1 stained with the biotinylated Aleuria aurantia lectin (AAL) ( B ) or with serum IgE from a patient with bee venom allergy (C) . Molecular weights are indicated with the molecular weight marker M.
FIG E1. A, Coomassie blue-stained SDS-PAGE showing nApi m 1 and rApi m 1. Nitrocellulose-blotted nApi m 1 and rApi m 1 stained with the biotinylated Aleuria aurantia lectin (AAL) ( B ) or with serum IgE from a patient with bee venom allergy (C) . Molecular weights are indicated with the molecular weight marker M.CC-BY · From the PDF
FIG E2. Correlation of levels of sIgE to rApi m 1 as determined by ImmunoCAP (kUA/L) and ELISA (OD) (Pearson correlation coefficient R 5 0.7453; P < .0005).
FIG E2. Correlation of levels of sIgE to rApi m 1 as determined by ImmunoCAP (kUA/L) and ELISA (OD) (Pearson correlation coefficient R 5 0.7453; P < .0005).CC-BY · From the PDF
FIG E3. Size exclusion chromatography of nApi m 1 ( A ) and rApi m 1 ( B ). Elution volumes of marker proteins (cytochrome C, 12 kDa; carbonic anhydrase, 29 kDa) are indicated by arrows. Shown are elution volumes (x-axis) and absorbance units (y-axis).
FIG E3. Size exclusion chromatography of nApi m 1 ( A ) and rApi m 1 ( B ). Elution volumes of marker proteins (cytochrome C, 12 kDa; carbonic anhydrase, 29 kDa) are indicated by arrows. Shown are elution volumes (x-axis) and absorbance units (y-axis).CC-BY · From the PDF

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Research works printed but not linked: 20

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Metadata

Authors
Gattinger, P., Bidovec-Stojkovic, U., Zidarn, M., Korosec, P., Valenta, R., & Mittermann, I.
Venue
Journal of Allergy and Clinical Immunology
Publisher
Elsevier BV
Published
2021-04
Volume
147
Issue
4
Pages
1502-1504.e5
ISSN
0091-6749
DOI
10.1016/j.jaci.2020.10.002
Cited by
12
References
0
Language
en
Licence
Funders
Austrian Science Fund

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CoChat. (2026). Citation check: Glycosylation enhances allergenic activity of major bee venom allergen Api m 1 by adding IgE epitopes. https://app.cochat.ai/papers/10.1016/j.jaci.2020.10.002
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Gattinger, P., Bidovec-Stojkovic, U., Zidarn, M., Korosec, P., Valenta, R., & Mittermann, I. (2021). Glycosylation enhances allergenic activity of major bee venom allergen Api m 1 by adding IgE epitopes. Journal of Allergy and Clinical Immunology. https://doi.org/10.1016/j.jaci.2020.10.002