Allergy to Mus m 1: Allergy to Mus m 1: A review of structural, and immunological features

Múnera, Marlon; Sánchez, Jorge; Sánchez, Jorge; M, Nordmann; Perez, Mariana; Aparicio, Dilia

doi:10.1016/j.imlet.2019.03.012

Cited by 7 publications

(6 citation statements)

References 27 publications

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“…Mouse sensitization and allergen exposure are associated with asthma severity, and mice were identified as the major allergen sources contributing to asthma morbidity in urban children in America. [20][21][22] Interestingly, no sensitization to pollen allergens was detected, which may be due to the young age of the cohort, but it is also possible that they are exposed to low allergenic grasses as was observed in a population from Asia. 23 Nearly 50% of the children without AD from rural communities had IgE antibodies against α-gal.…”

Section: Discussionmentioning

confidence: 88%

“…Interestingly, urban AD children showed significantly more sensitization to the mouse allergen Mus m 1 than rural AD children, which could be due to a more frequent exposure to mice and rats in the urban settings. Mouse sensitization and allergen exposure are associated with asthma severity, and mice were identified as the major allergen sources contributing to asthma morbidity in urban children in America 20‐22 …”

Section: Discussionmentioning

confidence: 99%

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Molecular IgE sensitization profiles of urban and rural children in South Africa

Mittermann

Dzoro

Gattinger

et al. 2020

Pediatric Allergy Immunology

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Background Allergens can act as disease‐triggering factors in atopic dermatitis (AD) patients. The aim of the study was to elucidate the molecular IgE sensitization profile in children with and without AD living in urban and rural areas of South Africa. Methods Specific IgE reactivity was assessed in 166 Black South African children aged 9‐38 months using a comprehensive panel of microarrayed allergens. According to clinical characterization children fell in four groups, urban AD cases (n = 32), urban controls (non‐AD, n = 40), rural cases (n = 49) and rural controls (non‐AD, n = 45). Results IgE reactivity to at least one of the allergens was detected in 94% of urban and 86% of rural AD children. House dust mite (HDM; 81% urban, 74% rural AD) and animal‐derived allergens (50% urban, 31% rural AD) were the most frequently recognized respiratory allergens, whereas IgE to pollen allergens was almost absent. Urban AD children showed significantly higher frequency of IgE reactivity (50%) to mouse lipocalin, Mus m 1, than rural AD children (12%). The most frequently recognized food allergens were from egg (63% urban, 43% rural AD), peanut (31% vs 41%), and soybean (22% vs 27%), whereas milk sensitization was rare. α‐gal‐specific IgE almost exclusively occurred in rural children (AD: 14%, non‐AD: 49%). Conclusion Molecular allergy diagnosis detects frequent IgE sensitization to HDM, animal but not pollen allergens and to egg, peanut, and soy, but not milk allergens in African AD children. Urban AD children reacted more often to Mus m 1, whereas α‐gal sensitization is more common in rural children likely due to parasite exposure.

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Section: Discussionmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Molecular IgE sensitization profiles of urban and rural children in South Africa

Mittermann

Dzoro

Gattinger

et al. 2020

Pediatric Allergy Immunology

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“…Overall, epitope predictions imply that rMus m 1.0102 has antigenic properties [ 44 ], a prerequisite for allergenicity and specific IgE-binding ability. Moreover, epitope III (predicted by Discotope 2.0) is shared by Rat n 1 and Equ c 1, which may explain the occurrence of cross-reacting sIgE in patients primarily allergic to mice [ 45 , 46 ]. Interestingly, among the residues involved in the predicted epitopes, E13, D34, and N35 correspond to residues which undergo substitution both in central ( Figure 1 A,B) and peripheral MUPs ( Figures S1 and S2 ); this fact reinforces the idea that rMus m 1.0102 may represent a component endowed with specific antigenicity.…”

Section: Discussionmentioning

confidence: 99%

Component-Resolved Diagnosis Based on a Recombinant Variant of Mus m 1 Lipocalin Allergen

Ferrari

Breda

Spisni

et al. 2023

IJMS

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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-structure. Conventional diagnosis of mouse allergy is based on serum IgE testing, using an epithelial extract as the antigen source. Given the heterogeneous and variable composition of extracts, we developed an indirect ELISA assay based on the recombinant component Mus m 1.0102. The assay performed with adequate precision and reasonable diagnostic accuracy (AUC = 0.87) compared to a routine clinical diagnostic test that exploits the native allergen. Recombinant Mus m 1.0102 turned out to be a valuable tool to study the fine epitope mapping of specific IgE reactivity to the major allergen responsible for mouse allergy. We believe that advancing in its functional characterization will lead to the standardization of murine lipocalins and to the development of allergen-specific immunotherapy.

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“…Initially considered a single protein, Mus m 1 is a complex of homologous pheromone-binding lipocalins, synthesized in the liver, called major urinary proteins (MUPs). 4,5 MUPs are expressed more in males than females, and more in adults than juveniles. 6 Mature MUPs are around 162 amino acids long and share a hydrophobic β-barrel that binds volatile small molecules for slow release, which facilitates their function as pheromones.…”

Section: Introductionmentioning

confidence: 97%

“…A 67 kDaputative allergen predominant in serum is albumin, and a 17–20 kDa allergen in serum and urine has been identified as Mus m 1. Initially considered a single protein, Mus m 1 is a complex of homologous pheromone‐binding lipocalins, synthesized in the liver, called major urinary proteins (MUPs) 4,5 . MUPs are expressed more in males than females, and more in adults than juveniles 6 .…”

Section: Introductionmentioning

confidence: 99%

Diversity and complexity of mouse allergens in urine, house dust, and allergen extracts assessed with an immuno‐allergomic approach

Mindaye¹,

Sun²,

Esfahani³

et al. 2021

Allergy

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Background: Mouse allergy is an important cause of indoor asthma and allergic rhinoconjunctivitis. The major mouse allergen, Mus m 1, is a complex of homologous pheromone-binding lipocalins called major urinary proteins (MUPs). Methods:We analyzed the proteome of MUPs in mouse urine, commercial mouse epithelial extracts, and environmental samples using several approaches. These include as follows: two-dimensional electrophoresis and immunoblotting; liquid chromatography-high-resolution mass spectrometry (LC/HRMS); multiple reaction monitoring (MRM) mass spectrometry; and LC/HRMS analysis of glycans at the N-66 residue of MUP3.Results: Albumin is predominant in the extracts, while MUPs are predominant in urine. LC/HRMS of 4 mouse allergen extracts revealed surprising heterogeneity. Of 22 known mouse MUPs, only 6 (MUP3, MUP4, MUP5, MUP13, MUP20, and MUP21) could be identified with MRM using unique peptides. Assessment of MUP content in urine, extracts, and dust samples showed good correlation between MRM and other methods working with different detection principles. All 6 identifiable MUPs were found in electrophoretically separated urine bands, but only MUP3 and MUP20 were above LOQ in unseparated mouse urine, and only MUP3, MUP4, and MUP20 were found in mouse epithelial extracts. Glycan heterogeneity was noted among 4 individual inbred mice: of 13 glycan structures detected, 8 were unique to one mouse, and only 2 glycan modifications were present in all 4 mice. Conclusions:Using mass spectrometry and MRM, mouse allergen extracts and urine samples are shown to be complex and heterogeneous. The efficacy and safety of commercial mouse allergen extracts will be improved with better controls of allergen content.

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Allergy to Mus m 1: Allergy to Mus m 1: A review of structural, and immunological features

Cited by 7 publications

References 27 publications

Molecular IgE sensitization profiles of urban and rural children in South Africa

Molecular IgE sensitization profiles of urban and rural children in South Africa

Component-Resolved Diagnosis Based on a Recombinant Variant of Mus m 1 Lipocalin Allergen

Diversity and complexity of mouse allergens in urine, house dust, and allergen extracts assessed with an immuno‐allergomic approach

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