2023
DOI: 10.3390/ijms24021193
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Component-Resolved Diagnosis Based on a Recombinant Variant of Mus m 1 Lipocalin Allergen

Abstract: Exposure to the Mus m 1 aeroallergen is a significant risk factor for laboratory animal allergy. This allergen, primarily expressed in mouse urine where it is characterized by a marked and dynamic polymorphism, is also present in epithelium and dander. Considering the relevance of sequence/structure assessment in protein antigenic reactivity, we compared the sequence of the variant Mus m 1.0102 to other members of the Mus m 1 allergen, and used Discotope 2.0 to predict conformational epitopes based on its 3D-s… Show more

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Cited by 4 publications
(5 citation statements)
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“…Figure S1 shows the results obtained from the analysis of the recombinant cat allergens via mass spectrometry. The theoretical molecular masses calculated for Fel d 1, Fel d 3, Fel d 4, Fel d 7 and Fel d 8, including the C-terminal hexa-histidine tags, were 18,942,11,864,20,664,19,302 and 24,766 Da, respectively. These calculated molecular masses were in good agreement with the masses determined via mass spectrometry (i.e., 19,128,11,695,20,639,19,687 and 24,719 Da) (Figure S1).…”
Section: Characterization Of Cat Allergen Moleculesmentioning
confidence: 94%
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“…Figure S1 shows the results obtained from the analysis of the recombinant cat allergens via mass spectrometry. The theoretical molecular masses calculated for Fel d 1, Fel d 3, Fel d 4, Fel d 7 and Fel d 8, including the C-terminal hexa-histidine tags, were 18,942,11,864,20,664,19,302 and 24,766 Da, respectively. These calculated molecular masses were in good agreement with the masses determined via mass spectrometry (i.e., 19,128,11,695,20,639,19,687 and 24,719 Da) (Figure S1).…”
Section: Characterization Of Cat Allergen Moleculesmentioning
confidence: 94%
“…The molecular characterization of disease-causing allergen molecules has received a strong boost through the application of molecular biological techniques for allergen characterization [17,18]. Today, the molecular structures of many important allergens have been determined, and recombinant allergens resembling the allergen repertoire of complex allergen sources are available, offering possibilities for improved molecular allergy diagnosis and molecular forms of immunotherapy [18,19]. Regarding cats, eight cat allergen molecules have been described and are recorded in the IUIS allergen database [20].…”
Section: Introductionmentioning
confidence: 99%
“…In addition, the presence of bioactive molecules (e.g., proteolytic enzymes) in natural extracts may affect the stability of the allergen extract. Contamination of the natural allergen extract with proteins from other sources is also possible [13][14][15][16][17][18][19].…”
Section: Extract-based and Component (Molecular) Immunological Allerg...mentioning
confidence: 99%
“…Almost all of these respiratory allergens have been characterized by dynamic markers using Western blotting, HPLc, and polymorphism, and have been identified by ELISA. Here, in addition we used IEDB Analysis Resource (Discotope 2.0) to predict the conformational epitopes of the heterogeneous molecules resulting from Mus m1, in order to standardize the murine lipocalin family [ 61 ].…”
Section: Proteomic Technologies For the Study Of Respiratory Allergiesmentioning
confidence: 99%