Purification and immunochemical characterization of Pla l 2, the profilin from Plantago lanceolata
Copyright © 2017 Elsevier Ltd. All rights reserved..
Profilins are small actin-binding proteins found in eukaryotes and involved in cell development, cytokinesis, membrane trafficking, and cell motility. From an allergenic point of view, profilins are panallergens usually involved in allergic polysensitization, although they are generally recognized as minor allergens. The objectives of this study were to identify and characterize the profilin from Plantago lanceolata pollen and to investigate the cross-reactivity between profilins from different pollen allergenic sources. Profilins from P. lancelolata (Pla l 2) and palm tree pollen (Pho d 2) were purified by affinity chromatography, deeply characterized and identified by mass spectrometry. Pla l 2 allergenicity was confirmed by immunoblot with serum samples from a patient population sensitized to profilin. Immunoblot inhibition was performed to study IgG reactivity between different pollen profilins. IgE cross-reactivity was demonstrated by ImmunoCAP inhibition. Pla l 2 is the second P. lanceolata allergen included in the IUIS Allergen Nomenclature database. Four peptides from purified Pla l 2 were identified with percentages of homology with other pollen profilins between 73 and 86%. Eighty-six percent (21/24) of the patient population recognized Pla l 2. The allergenic relatedness between Pla l 2, Pho d 2 and six pollen profilins was confirmed, and IgE cross-reactivity of Pla l 2 with rBet v 2 and rPhl p 12 was demonstrated. Pla l 2 is the profilin from P. lanceolata. The demonstrated allergenicity of this protein and its cross-reactivity with other pollen profilins support its use in profilin diagnostic assays.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2017 |
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| Erschienen: |
2017 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:83 |
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| Enthalten in: |
Molecular immunology - 83(2017) vom: 30. März, Seite 100-106 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Moya, Raquel [VerfasserIn] |
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| Links: |
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| Themen: |
Allergens |
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| Anmerkungen: |
Date Completed 11.09.2017 Date Revised 21.02.2018 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.molimm.2017.01.017 |
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| Förderinstitution / Projekttitel: |
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NLM268376093 |
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| 245 | 1 | 0 | |a Purification and immunochemical characterization of Pla l 2, the profilin from Plantago lanceolata |
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| 500 | |a Date Revised 21.02.2018 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2017 Elsevier Ltd. All rights reserved. | ||
| 520 | |a Profilins are small actin-binding proteins found in eukaryotes and involved in cell development, cytokinesis, membrane trafficking, and cell motility. From an allergenic point of view, profilins are panallergens usually involved in allergic polysensitization, although they are generally recognized as minor allergens. The objectives of this study were to identify and characterize the profilin from Plantago lanceolata pollen and to investigate the cross-reactivity between profilins from different pollen allergenic sources. Profilins from P. lancelolata (Pla l 2) and palm tree pollen (Pho d 2) were purified by affinity chromatography, deeply characterized and identified by mass spectrometry. Pla l 2 allergenicity was confirmed by immunoblot with serum samples from a patient population sensitized to profilin. Immunoblot inhibition was performed to study IgG reactivity between different pollen profilins. IgE cross-reactivity was demonstrated by ImmunoCAP inhibition. Pla l 2 is the second P. lanceolata allergen included in the IUIS Allergen Nomenclature database. Four peptides from purified Pla l 2 were identified with percentages of homology with other pollen profilins between 73 and 86%. Eighty-six percent (21/24) of the patient population recognized Pla l 2. The allergenic relatedness between Pla l 2, Pho d 2 and six pollen profilins was confirmed, and IgE cross-reactivity of Pla l 2 with rBet v 2 and rPhl p 12 was demonstrated. Pla l 2 is the profilin from P. lanceolata. The demonstrated allergenicity of this protein and its cross-reactivity with other pollen profilins support its use in profilin diagnostic assays | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Cross-reactivity | |
| 650 | 4 | |a Molecular diagnosis | |
| 650 | 4 | |a Panallergen | |
| 650 | 4 | |a Plantago lanceolata | |
| 650 | 4 | |a Profilin | |
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| 650 | 7 | |a Antigens, Plant |2 NLM | |
| 650 | 7 | |a Glycoproteins |2 NLM | |
| 650 | 7 | |a Plant Proteins |2 NLM | |
| 650 | 7 | |a Profilins |2 NLM | |
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| 700 | 1 | |a Beitia, Juan Mª |e verfasserin |4 aut | |
| 700 | 1 | |a Carnés, Jerónimo |e verfasserin |4 aut | |
| 700 | 1 | |a López-Matas, M Angeles |e verfasserin |4 aut | |
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