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Article ; Online: Component-Resolved Diagnosis Based on a Recombinant Variant of Mus m 1 Lipocalin Allergen.

Ferrari, Elena / Breda, Daniela / Spisni, Alberto / Burastero, Samuele E

International journal of molecular sciences

2023 Volume 24, Issue 2

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. ... ...

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-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.
MeSH term(s)	Animals ; Mice ; Allergens ; Lipocalins/genetics ; Food Hypersensitivity ; Enzyme-Linked Immunosorbent Assay ; Immunoglobulin E ; Recombinant Proteins/genetics
Chemical Substances	Allergens ; Lipocalins ; Immunoglobulin E (37341-29-0) ; Recombinant Proteins
Language	English
Publishing date	2023-01-07
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24021193
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Article ; Online: T-cell receptor-mediated cross-reactivity to different allergens is driven by recognition of homologous, phylogenetically conserved epitopes.

Burastero, Samuele E

The Journal of allergy and clinical immunology

2016 Volume 138, Issue 4, Page(s) 1237

MeSH term(s)	Allergens ; Amino Acid Sequence ; Antigens, Plant ; Cross Reactions ; Epitopes ; Plant Proteins ; Receptors, Antigen, T-Cell
Chemical Substances	Allergens ; Antigens, Plant ; Epitopes ; Plant Proteins ; Receptors, Antigen, T-Cell
Language	English
Publishing date	2016-07-30
Publishing country	United States
Document type	Letter ; Comment
ZDB-ID	121011-7
ISSN	1097-6825 ; 1085-8725 ; 0091-6749
ISSN (online)	1097-6825 ; 1085-8725
ISSN	0091-6749
DOI	10.1016/j.jaci.2016.04.055
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Article: Serological proteome analysis identifies crustacean myosin heavy chain type 1 protein and house dust mite Der p 14 as cross-reacting allergens.

Conti, Antonio / Alqassir, Noor / Breda, Daniela / Zanardi, Alan / Alessio, Massimo / Burastero, Samuele E

Advances in clinical and experimental medicine : official organ Wroclaw Medical University

2023 Volume 32, Issue 1, Page(s) 107–112

Abstract: Background: Allergies to house dust mite (HDM) and to crustaceans are clinically and pathogenically linked. Several homologous allergenic proteins have been identified, among which tropomyosin is the prototype, expressing epitopes endowed with variable ... ...

Abstract	Background: Allergies to house dust mite (HDM) and to crustaceans are clinically and pathogenically linked. Several homologous allergenic proteins have been identified, among which tropomyosin is the prototype, expressing epitopes endowed with variable levels of immunoglobulin E (IgE) cross-reactivity. Component-resolved diagnosis (CRD) does not allow a thorough characterization of all relevant IgE reactivities to these allergen sources. Objectives: We studied 1 patient allergic to shrimp with positive skin prick test to HDM and negative scores for IgE to HDM allergen components routinely used in CRD (group 1 and 2 allergens, Der p 23 and tropomyosin). Material and methods: In order to identify the allergen(s) involved in IgE reactivity, we used serological proteome analysis (SERPA), which utilizes two-dimensional gel electrophoresis (2DE), immunoblotting and mass spectrometry (MS). The identified allergenic proteins were tested with sera from 20 crustacean-allergic patients and 19 grass-allergic patients serving as controls. Results: Der p 14 and myosin heavy chain type 1 (MHC1) were identified as the components recognized by patient's IgE in the proteome of Dermatophagoides pteronyssinus and Penaeus monodon, respectively. The MHC1 protein shows about 30% sequence identity with Der p 14 in specific domains, and cross-reactivity against epitopes shared by the 2 proteins was demonstrated by reduced reactivity to shrimp extract following pre-incubation with Der p 14. Serum IgE from 5 out of 20 patients allergic to crustaceans reacted with MHC1, compared to none among 19 controls (p < 0.05). Conclusion: We identified MHC1 as a relevant allergic component in the proteome of Penaeus monodon, the prototypic allergen source used in diagnosis of allergy to crustaceans. Our data demonstrate MHC1 cross-reactivity between MHC1 and Der p 14 from Dermatophagoides pteronyssinus.
MeSH term(s)	Animals ; Humans ; Allergens ; Epitopes/chemistry ; Hypersensitivity ; Immunoglobulin E ; Myosin Heavy Chains ; Proteome ; Pyroglyphidae ; Tropomyosin/chemistry ; Shellfish Hypersensitivity ; Cross Reactions
Chemical Substances	Allergens ; Epitopes ; Immunoglobulin E (37341-29-0) ; Myosin Heavy Chains (EC 3.6.4.1) ; Proteome ; Tropomyosin
Language	English
Publishing date	2023-01-07
Publishing country	Poland
Document type	Journal Article
ZDB-ID	2270257-X
ISSN	1899-5276 ; 1230-025X
ISSN	1899-5276 ; 1230-025X
DOI	10.17219/acem/158773
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Article: Periostin expression in uninvolved skin as a potential biomarker for rapid cutaneous progression in systemic sclerosis patients: a preliminary explorative study.

De Luca, Giacomo / Campochiaro, Corrado / Burastero, Samuele E / Matucci-Cerinic, Marco / Doglioni, Claudio / Dagna, Lorenzo

Frontiers in medicine

2024 Volume 10, Page(s) 1214523

Abstract: Objectives: This study aimed to evaluate periostin serum levels and skin expression in patients with systemic sclerosis (SSc).: Methods: We enrolled 35 patients with diffuse (d-SSc) or limited (l-SSc) SSc, 15 patients with very early diagnosis of ... ...

Abstract	Objectives: This study aimed to evaluate periostin serum levels and skin expression in patients with systemic sclerosis (SSc). Methods: We enrolled 35 patients with diffuse (d-SSc) or limited (l-SSc) SSc, 15 patients with very early diagnosis of systemic sclerosis (VEDOSS), and 30 sex-matched healthy controls. Periostin serum levels were determined by an enzyme-linked immunosorbent assay (ELISA). Periostin skin expression was determined by immunohistochemistry (IHC) on paired involved and uninvolved 5-mm skin biopsy samples in a subgroup of 10 d-SSc and 10 L-SSc patients. A 12-month follow-up was considered. Results: We included 50 patients (mean age 53.1 ± 16.1 years; women 94%; mean disease duration 38.2 ± 45.1 months; anti-centromere 50%; anti-Scl70 40%), 35 of them with a definite SSc (68.8% l-SSc; 31.4% d-SSc; mean mRSS 9.0 ± 7.2) and 15 with VEDOSS; 30 controls were also included in this study. Periostin serum levels were higher in SSc patients compared to controls (32.7 ± 8.0 ng/mL vs. 27.7 ± 7.3 ng/mL; Conclusion: Periostin skin expression may be a useful biomarker to indicate the presence of a disease at a higher risk of rapid cutaneous involvement.
Language	English
Publishing date	2024-01-24
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2775999-4
ISSN	2296-858X
ISSN	2296-858X
DOI	10.3389/fmed.2023.1214523
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Article: Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants

Ferrari, Elena / Corsini, Romina / Burastero, Samuele E. / Tanfani, Fabio / Spisni, Alberto

Data in Brief. 2020 Apr., v. 29

2020

Abstract: The presented data were obtained with the lipocalin allergen Mus m 1.0102 and its cysteine mutants MM-C138A, MM-C157A and MM-C138,157A, whose structural features and unfold reversibility investigations are presented in the research article entitled “The ... ...

Abstract	The presented data were obtained with the lipocalin allergen Mus m 1.0102 and its cysteine mutants MM-C138A, MM-C157A and MM-C138,157A, whose structural features and unfold reversibility investigations are presented in the research article entitled “The allergen Mus m 1.0102: cysteine residues and molecular allergology” [1].The data were obtained by means of a Dynamic Light Scattering-based thermal stability assay, a Fluorescence-based ligand-binding assay and a basophil degranulation test, and describe proteins’ fold stability, ligand binding ability and allergenic potential, respectively. Analysis of the collected data produced the temperatures corresponding to the onset of the protein unfolding, the dissociation constants for N-Phenyl-1-naphthylamine ligand and the profiles of β-hexosaminidase release from RBL SX-38 cells, sensitized with the serum of selected allergic patients and incubated with increasing antigens concentrations.These data allow for comparison of the lipocalin allergen Mus m 1.0102 with its conserved cysteines mutants and, with regard to their potential application in allergy diagnostics and immunotherapy, they contribute to the process of recombinant allergen characterization and standardization.
Keywords	allergenicity ; allergens ; blood serum ; cysteine ; diagnostic techniques ; dissociation ; hypersensitivity ; immunotherapy ; ligands ; thermal stability
Language	English
Dates of publication	2020-04
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	2786545-9
ISSN	2352-3409
ISSN	2352-3409
DOI	10.1016/j.dib.2020.105355
Database	NAL-Catalogue (AGRICOLA)

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Article: The allergen Mus m 1.0102: Cysteine residues and molecular allergology

Ferrari, Elena / Corsini, Romina / Burastero, Samuele E / Tanfani, Fabio / Spisni, Alberto

Molecular immunology. 2020 Apr., v. 120

2020

Abstract: Mus m 1.0102 is a member of the mouse Major Urinary Protein family, belonging to the Lipocalins superfamily. Major Urinary Proteins (MUPs) are characterized by highly conserved structural motifs. These include a disulphide bond, involved in protein ... ...

Abstract	Mus m 1.0102 is a member of the mouse Major Urinary Protein family, belonging to the Lipocalins superfamily. Major Urinary Proteins (MUPs) are characterized by highly conserved structural motifs. These include a disulphide bond, involved in protein oxidative folding and protein structure stabilization, and a free cysteine residue, substituted by serine only in the pheromonal protein Darcin (MUP20). The free cysteine is recognized as responsible for the onset of inter- or intramolecular thiol/disulphide exchange, an event that favours protein aggregation.Here we show that the substitution of selected cysteine residues modulates Mus m 1.0102 protein folding, fold stability and unfolding reversibility, while maintaining its allergenic potency.Recombinant allergens used for immunotherapy or employed in allergy diagnostic kits require, as essential features, conformational stability, sample homogeneity and proper immunogenicity. In this perspective, recombinant Mus m 1.0102 might appear reasonably adequate as lead molecule because of its allergenic potential and thermal stability. However, its modest resistance to aggregation renders the protein unsuitable for pharmacological preparations. Point mutation is considered a winning strategy.We report that, among the tested mutants, C138A mutant acquires a structure more resistant to thermal stress and less prone to aggregation, two events that act positively on the protein shelf life. Those features make that MUP variant an attractive lead molecule for the development of a diagnostic kit and/or a vaccine.
Keywords	Mus ; allergenicity ; allergens ; alpha-globulins ; analytical kits ; cysteine ; disulfide bonds ; disulfides ; hypersensitivity ; immunogenicity ; immunotherapy ; mutants ; point mutation ; protein folding ; serine ; shelf life ; thermal stability ; thermal stress ; thiols ; vaccines
Language	English
Dates of publication	2020-04
Size	p. 1-12.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2020.01.022
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Thermal stability, ligand binding and allergenicity data of Mus m 1.0102 allergen and its cysteine mutants.

Ferrari, Elena / Corsini, Romina / Burastero, Samuele E / Tanfani, Fabio / Spisni, Alberto

Data in brief

2020 Volume 29, Page(s) 105355

Abstract	The presented data were obtained with the lipocalin allergen Mus m 1.0102 and its cysteine mutants MM-C138A, MM-C157A and MM-C138,157A, whose structural features and unfold reversibility investigations are presented in the research article entitled "The allergen Mus m 1.0102: cysteine residues and molecular allergology" [1]. The data were obtained by means of a Dynamic Light Scattering-based thermal stability assay, a Fluorescence-based ligand-binding assay and a basophil degranulation test, and describe proteins' fold stability, ligand binding ability and allergenic potential, respectively. Analysis of the collected data produced the temperatures corresponding to the onset of the protein unfolding, the dissociation constants for N-Phenyl-1-naphthylamine ligand and the profiles of β-hexosaminidase release from RBL SX-38 cells, sensitized with the serum of selected allergic patients and incubated with increasing antigens concentrations. These data allow for comparison of the lipocalin allergen Mus m 1.0102 with its conserved cysteines mutants and, with regard to their potential application in allergy diagnostics and immunotherapy, they contribute to the process of recombinant allergen characterization and standardization.
Language	English
Publishing date	2020-02-29
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2786545-9
ISSN	2352-3409 ; 2352-3409
ISSN (online)	2352-3409
ISSN	2352-3409
DOI	10.1016/j.dib.2020.105355
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Article ; Online: The allergen Mus m 1.0102: Cysteine residues and molecular allergology.

Ferrari, Elena / Corsini, Romina / Burastero, Samuele E / Tanfani, Fabio / Spisni, Alberto

Molecular immunology

2020 Volume 120, Page(s) 1–12

Abstract	Mus m 1.0102 is a member of the mouse Major Urinary Protein family, belonging to the Lipocalins superfamily. Major Urinary Proteins (MUPs) are characterized by highly conserved structural motifs. These include a disulphide bond, involved in protein oxidative folding and protein structure stabilization, and a free cysteine residue, substituted by serine only in the pheromonal protein Darcin (MUP20). The free cysteine is recognized as responsible for the onset of inter- or intramolecular thiol/disulphide exchange, an event that favours protein aggregation. Here we show that the substitution of selected cysteine residues modulates Mus m 1.0102 protein folding, fold stability and unfolding reversibility, while maintaining its allergenic potency. Recombinant allergens used for immunotherapy or employed in allergy diagnostic kits require, as essential features, conformational stability, sample homogeneity and proper immunogenicity. In this perspective, recombinant Mus m 1.0102 might appear reasonably adequate as lead molecule because of its allergenic potential and thermal stability. However, its modest resistance to aggregation renders the protein unsuitable for pharmacological preparations. Point mutation is considered a winning strategy. We report that, among the tested mutants, C138A mutant acquires a structure more resistant to thermal stress and less prone to aggregation, two events that act positively on the protein shelf life. Those features make that MUP variant an attractive lead molecule for the development of a diagnostic kit and/or a vaccine.
MeSH term(s)	Allergens/chemistry ; Allergens/genetics ; Allergens/immunology ; Amino Acid Substitution ; Animals ; Cell Line ; Cysteine/chemistry ; Humans ; Immunologic Tests ; Ligands ; Mice ; Models, Molecular ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Folding ; Protein Stability ; Protein Structure, Secondary ; Proteins/chemistry ; Proteins/genetics ; Proteins/immunology ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Spectrometry, Fluorescence ; Spectroscopy, Fourier Transform Infrared
Chemical Substances	Allergens ; Ligands ; Mus m 1 allergen, Mus musculus ; Proteins ; Recombinant Proteins ; major urinary proteins ; Cysteine (K848JZ4886)
Language	English
Publishing date	2020-02-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2020.01.022
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Article: Pollen-cross allergenicity mediated by panallergens: a clue to the patho-genesis of multiple sensitizations.

Burastero, Samuele E

Inflammation & allergy drug targets

2006 Volume 5, Issue 4, Page(s) 203–209

Abstract: Allergens are proteins capable of raising in predisposed (atopic) individuals an IgE-dependent type I hyper-sensitivity reaction, supporting allergic symptoms such as anaphylactic shock, asthma and rhinitis. Panallergens are evolutionarily conserved, ... ...

Abstract	Allergens are proteins capable of raising in predisposed (atopic) individuals an IgE-dependent type I hyper-sensitivity reaction, supporting allergic symptoms such as anaphylactic shock, asthma and rhinitis. Panallergens are evolutionarily conserved, ubiquitous components of several complex sources of allergens, which usually act as minor allergens, i.e., they do not react with the majority of sera from patients allergic to a given allergen source. However, their presence has important clinical implications in establishing the phenomenon of food-pollen cross-reactivity, in the interpretation of diagnostic tests and in the preparation of immunotherapy extracts. A T-lymphocyte component is necessary to support the panallergen-specific humoral IgE antibody response. While several excellent reviews are available regarding allergen cross-reactivity from the IgE-perspective, data on cross-allergenicity from the T-lymphocyte standpoint are quite limited. Indeed, this is a crucial issue in the comprehension of polysensitization, since it is the initial exposure to conserved panallergens that may subsequently drive the allergic immune response towards major allergenic components, which at first proved non-sensitizing to a given patient, through a mechanism of intermolecular epitope spreading. Here, we will discuss data showing that a functionally relevant T-cell response to molecularly defined, conserved regions of panallergens can support cross-allergenicity in allergic patients. This subject is relevant to the comprehension of the natural history and to the clinical management of the majority of allergic patients, who suffer from multiple allergies.
MeSH term(s)	Allergens/genetics ; Allergens/immunology ; Amino Acid Sequence ; Animals ; Cross Reactions ; Epitopes/immunology ; Humans ; Immunoglobulin E/immunology ; Molecular Sequence Data ; Plants/genetics ; Pollen/genetics ; Pollen/immunology ; T-Lymphocytes/immunology
Chemical Substances	Allergens ; Epitopes ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2006-12-12
Publishing country	United Arab Emirates
Document type	Journal Article ; Review
ZDB-ID	2215862-5
ISSN	2212-4055 ; 1871-5281
ISSN (online)	2212-4055
ISSN	1871-5281
DOI	10.2174/187152806779010918
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Article ; Online: Sublingual immunotherapy for allergic rhinitis: an update.

Burastero, Samuele E

Current opinion in otolaryngology & head and neck surgery

2006 Volume 14, Issue 3, Page(s) 197–201

Abstract: Purpose of review: The inter-relationship between allergy and nasal diseases has long been known. Failure to address when allergy is a contributing factor diminishes the possibility of a successful surgical intervention. Sublingual immunotherapy is ... ...

Abstract	Purpose of review: The inter-relationship between allergy and nasal diseases has long been known. Failure to address when allergy is a contributing factor diminishes the possibility of a successful surgical intervention. Sublingual immunotherapy is recommended by the World Health Organization to treat allergic rhinitis and is widely used in Europe. Many clinical trials and rigorous meta-analysis support its efficacy. The criteria, however, for the integration of this treatment (with the surgical management of those allergic patients who suffer chronic nasal obstruction, severe drug-resistant hypertrophy and increase in glandular structures of the inferior turbinates) are not fully established. We review here the most recent literature on the efficacy and safety of sublingual immunotherapy. The purpose is to stimulate the use of complementary approaches by ear, nose and throat doctors and allergologists, and to improve the management of patients with persistent allergic rhinitis. Recent findings: In addition to the results of clinical trials, postmarketing surveillance has confirmed the high safety profile of sublingual immunotherapy in adults and children, its positive impact on the quality of life, and the reduction of the personal and social cost of allergy. Sublingual immunotherapy can prevent new allergic sensitizations and maintain its beneficial effect for years after its discontinuation. Summary: Sublingual immunotherapy is a highly efficacious and well tolerated form of immunotherapy for allergic rhinitis, and it is capable of interfering with disease progression. Sublingual immunotherapy should be integrated with surgical intervention to achieve optimal outcomes in allergic subjects with chronic nasal obstruction.
MeSH term(s)	Administration, Sublingual ; Humans ; Immunotherapy ; Rhinitis, Allergic, Perennial/drug therapy ; Rhinitis, Allergic, Seasonal/drug therapy
Language	English
Publishing date	2006-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	1232518-1
ISSN	1531-6998 ; 1068-9508
ISSN (online)	1531-6998
ISSN	1068-9508
DOI	10.1097/01.moo.0000193187.23063.ae
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