LIVIVO - Search results -

Search results

Result 1 - 10 of total 119

Search options

Article ; Online: Cockroach allergy: Understanding complex immune responses to develop novel therapies.

Pomés, Anna / Arruda, L Karla

2023 Volume 156, Page(s) 157–169

Abstract: Cockroach allergy is associated with the development of asthma. The identification of cockroach allergens, which began in the 1990 s, is an ongoing process that has led to the current listing of 20 official allergen groups in the WHO/IUIS Allergen ... ...

Abstract	Cockroach allergy is associated with the development of asthma. The identification of cockroach allergens, which began in the 1990 s, is an ongoing process that has led to the current listing of 20 official allergen groups in the WHO/IUIS Allergen Nomenclature database. The function and structure of some of these allergens has been determined and define their natural delivery into the environment and their allergenicity. Analysis of antigenic determinants by X-ray crystallography and rational design of site-directed mutagenesis led to the identification of IgE binding sites for the design of molecules with reduced IgE reactivity and T cell modulatory capacity. New developments in recent years include component analyses of B and T cell reactivity and a recent cockroach immunotherapy trial, CRITICAL, that will contribute to understand the immune response to cockroach and to define future directions for cockroach allergy diagnosis and immunotherapy.
MeSH term(s)	Animals ; Immunoglobulin E ; Allergens ; Asthma/therapy ; Cockroaches ; Immunity
Chemical Substances	Immunoglobulin E (37341-29-0) ; Allergens
Language	English
Publishing date	2023-03-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2023.03.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 166: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Precision engineering for localization, validation, and modification of allergenic epitopes.

Pomés, Anna / Smith, Scott A / Chruszcz, Maksymilian / Mueller, Geoffrey A / Brackett, Nicole F / Chapman, Martin D

The Journal of allergy and clinical immunology

2024 Volume 153, Issue 3, Page(s) 560–571

Abstract: The allergen-IgE interaction is essential for the genesis of allergic responses, yet investigation of the molecular basis of these interactions is in its infancy. Precision engineering has unveiled the molecular features of allergen-antibody interactions ...

Abstract	The allergen-IgE interaction is essential for the genesis of allergic responses, yet investigation of the molecular basis of these interactions is in its infancy. Precision engineering has unveiled the molecular features of allergen-antibody interactions at the atomic level. High-resolution technologies, including x-ray crystallography, nuclear magnetic resonance spectroscopy, and cryo-electron microscopy, determine allergen-antibody structures. X-ray crystallography of an allergen-antibody complex localizes in detail amino acid residues and interactions that define the epitope-paratope interface. Multiple structures involving murine IgG mAbs have recently been resolved. The number of amino acids forming the epitope broadly correlates with the epitope area. The production of human IgE mAbs from B cells of allergic subjects is an exciting recent development that has for the first time enabled an actual IgE epitope to be defined. The biologic activity of defined IgE epitopes can be validated in vivo in animal models or by measuring mediator release from engineered basophilic cell lines. Finally, gene-editing approaches using the Clustered Regularly Interspaced Short Palindromic Repeats technology to either remove allergen genes or make targeted epitope engineering at the source are on the horizon. This review presents an overview of the identification and validation of allergenic epitopes by precision engineering.
MeSH term(s)	Mice ; Humans ; Animals ; Allergens ; Epitopes ; Plant Proteins ; Cryoelectron Microscopy ; Amino Acid Sequence ; Immunoglobulin E ; Antibodies, Monoclonal
Chemical Substances	Allergens ; Epitopes ; Plant Proteins ; Immunoglobulin E (37341-29-0) ; Antibodies, Monoclonal
Language	English
Publishing date	2024-01-03
Publishing country	United States
Document type	Journal Article ; Review
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.2023.12.017
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uh III Zs.92: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: New Frontiers: Precise Editing of Allergen Genes Using CRISPR.

Brackett, Nicole F / Pomés, Anna / Chapman, Martin D

Frontiers in allergy

2022 Volume 2, Page(s) 821107

Abstract: Genome engineering with clustered regularly interspaced short palindromic repeats (CRISPR) technology offers the unique potential for unequivocally deleting allergen genes at the source. Compared to prior gene editing approaches, CRISPR boasts ... ...

Abstract	Genome engineering with clustered regularly interspaced short palindromic repeats (CRISPR) technology offers the unique potential for unequivocally deleting allergen genes at the source. Compared to prior gene editing approaches, CRISPR boasts substantial improvements in editing efficiency, throughput, and precision. CRISPR has demonstrated success in several clinical applications such as sickle cell disease and β-thalassemia, and preliminary knockout studies of allergenic proteins using CRISPR editing show promise. Given the advantages of CRISPR, as well as specific DNA targets in the allergen genes, CRISPR gene editing is a viable approach for tackling allergy, which may lead to significant disease improvement. This review will highlight recent applications of CRISPR editing of allergens, particularly cat allergen Fel d 1, and will discuss the advantages and limitations of this approach compared to existing treatment options.
Language	English
Publishing date	2022-01-17
Publishing country	Switzerland
Document type	Journal Article ; Review
ISSN	2673-6101
ISSN (online)	2673-6101
DOI	10.3389/falgy.2021.821107
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- Full text online
- Order with fees

Article ; Online: Cross-reactivity in allergy: A double-edged sword.

Pomés, Anna / Schulten, Véronique

Allergy

2019 Volume 75, Issue 1, Page(s) 9–11

MeSH term(s)	Adaptive Immunity/immunology ; Ambrosia/immunology ; Cross Reactions ; Humans ; Hypersensitivity, Immediate/immunology
Language	English
Publishing date	2019-05-08
Publishing country	Denmark
Document type	Editorial ; Research Support, N.I.H., Extramural
ZDB-ID	391933-x
ISSN	1398-9995 ; 0105-4538
ISSN (online)	1398-9995
ISSN	0105-4538
DOI	10.1111/all.13993
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uh III Zs.150: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 125: Show issues

Order via subito

Details ▾

Article ; Online: Human Monoclonal IgE Antibodies-a Major Milestone in Allergy.

Smith, Scott A / Chruszcz, Maksymilian / Chapman, Martin D / Pomés, Anna

Current allergy and asthma reports

2022 Volume 23, Issue 1, Page(s) 53–65

Abstract: Purpose of review: Bound to its high affinity receptor on mast cells and basophils, the IgE antibody molecule plays an integral role in the allergic reaction. Through interactions with the allergen, it provides the sensitivity and specificity parameters ...

Abstract	Purpose of review: Bound to its high affinity receptor on mast cells and basophils, the IgE antibody molecule plays an integral role in the allergic reaction. Through interactions with the allergen, it provides the sensitivity and specificity parameters for cell activation and mediator release that produce allergic symptoms. Advancements in human hybridoma technologies allow for the generation and molecular definition of naturally occurring allergen-specific human IgE monoclonal antibodies. Recent findings: A high-resolution structure of dust mite allergen Der p 2 in complex with Fab of the human IgE mAb 2F10 was recently determined using X-ray crystallography. The structure reveals the fine molecular details of IgE 2F10 binding its 750 Å
MeSH term(s)	Humans ; Immunoglobulin E ; Hypersensitivity ; Antibodies, Monoclonal/therapeutic use ; Epitopes/chemistry ; Allergens
Chemical Substances	Immunoglobulin E (37341-29-0) ; Antibodies, Monoclonal ; Epitopes ; Allergens
Language	English
Publishing date	2022-12-02
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	2057370-4
ISSN	1534-6315 ; 1529-7322
ISSN (online)	1534-6315
ISSN	1529-7322
DOI	10.1007/s11882-022-01055-w
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 5548: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Structural Aspects of the Allergen-Antibody Interaction.

Pomés, Anna / Mueller, Geoffrey A / Chruszcz, Maksymilian

Frontiers in immunology

2020 Volume 11, Page(s) 2067

Abstract: The development of allergic disease involves the production of IgE antibodies upon allergen exposure in a process called sensitization. IgE binds to receptors on the surface of mast cells and basophils, and subsequent allergen exposure leads to cross- ... ...

Abstract	The development of allergic disease involves the production of IgE antibodies upon allergen exposure in a process called sensitization. IgE binds to receptors on the surface of mast cells and basophils, and subsequent allergen exposure leads to cross-linking of IgE antibodies and release of cell mediators that cause allergy symptoms. Although this process is quite well-understood, very little is known about the epitopes on the allergen recognized by IgE, despite the importance of the allergen-antibody interaction for the allergic response to occur. This review discusses efforts to analyze allergen-antibody interactions, from the original epitope mapping studies using linear peptides or recombinant allergen fragments, to more sophisticated technologies, such as X-ray crystallography and nuclear magnetic resonance. These state-of-the-art approaches, combined with site-directed mutagenesis, have led to the identification of conformational IgE epitopes. The first structures of an allergen (egg lysozyme) in complex with Fab fragments from IgG antibodies were determined in the 1980s. Since then, IgG has been used as surrogate for IgE, due to the difficulty of obtaining monoclonal IgE antibodies. Technical developments including phage display libraries have contributed to progress in epitope mapping thanks to the isolation of IgE antibody constructs from combinatorial libraries made from peripheral blood mononuclear cells of allergic donors. Most recently, single B cell antibody sequencing and human hybridomas are new breakthrough technologies for finally obtaining human IgE monoclonal antibodies, ideal for epitope mapping. The information on antigenic determinants will facilitate the design of hypoallergens for immunotherapy and the investigation of the fundamental mechanisms of the IgE response.
MeSH term(s)	Allergens/chemistry ; Allergens/immunology ; Animals ; Antibodies/chemistry ; Antibodies/immunology ; Antigen-Antibody Complex/chemistry ; Antigen-Antibody Complex/immunology ; Antigen-Antibody Reactions/immunology ; Crystallography, X-Ray ; Epitope Mapping/methods ; Epitopes/immunology ; Humans ; Immunoglobulin E/immunology ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Protein Binding ; Structure-Activity Relationship
Chemical Substances	Allergens ; Antibodies ; Antigen-Antibody Complex ; Epitopes ; Immunoglobulin E (37341-29-0)
Keywords	covid19
Language	English
Publishing date	2020-09-02
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2020.02067
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Quantification of peanut allergens across recalled and nonrecalled lots of diagnostic peanut extracts.

Stone, Cosby A / Hemler, Jonathan A / Filep, Stephanie / Braden, Karen / Pomés, Anna / Chapman, Martin D / Smith, Scott A

The journal of allergy and clinical immunology. In practice

2023 Volume 11, Issue 11, Page(s) 3547–3549.e1

MeSH term(s)	Humans ; Allergens ; Arachis ; Antigens, Plant ; Plant Proteins ; Peanut Hypersensitivity/diagnosis
Chemical Substances	Allergens ; Antigens, Plant ; Plant Proteins
Language	English
Publishing date	2023-07-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2843237-X
ISSN	2213-2201 ; 2213-2198
ISSN (online)	2213-2201
ISSN	2213-2198
DOI	10.1016/j.jaip.2023.07.015
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 7086: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Evolutionary Biology and Gene Editing of Cat Allergen, Fel d 1.

Brackett, Nicole F / Davis, Brian W / Adli, Mazhar / Pomés, Anna / Chapman, Martin D

The CRISPR journal

2022 Volume 5, Issue 2, Page(s) 213–223

Abstract: Allergy to domestic cat affects up to 15% of the population, and sensitization to cat allergen is associated with asthma. Despite the pervasiveness of cat allergic disease, current treatments have limited impact. Here, we present a bioinformatics ... ...

Abstract	Allergy to domestic cat affects up to 15% of the population, and sensitization to cat allergen is associated with asthma. Despite the pervasiveness of cat allergic disease, current treatments have limited impact. Here, we present a bioinformatics analysis of the major cat allergen, Fel d 1, and demonstrate proof of principle for CRISPR gene editing of the allergen. Sequence and structural analyses of Fel d 1 from 50 domestic cats identified conserved coding regions in genes
MeSH term(s)	Allergens/chemistry ; Allergens/genetics ; Animals ; Biology ; CRISPR-Cas Systems/genetics ; Cats ; Gene Editing ; Glycoproteins/chemistry ; Glycoproteins/genetics ; Hypersensitivity/genetics ; Hypersensitivity/therapy
Chemical Substances	Allergens ; Glycoproteins
Language	English
Publishing date	2022-03-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3017891-5
ISSN	2573-1602 ; 2573-1599
ISSN (online)	2573-1602
ISSN	2573-1599
DOI	10.1089/crispr.2021.0101
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 7195: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MG 119: Show issues

Order via subito

Details ▾

Article ; Online: Structural and ligand binding analysis of the pet allergens Can f 1 and Fel d 7.

Min, Jungki / Foo, Alexander C Y / Gabel, Scott A / Perera, Lalith / DeRose, Eugene F / Pomés, Anna / Pedersen, Lars C / Mueller, Geoffrey A

Frontiers in allergy

2023 Volume 4, Page(s) 1133412

Abstract: Introduction: Pet lipocalins are respiratory allergens with a central hydrophobic ligand-binding cavity called a calyx. Molecules carried in the calyx by allergens are suggested to influence allergenicity, but little is known about the native ligands.!## ...

Abstract	Introduction: Pet lipocalins are respiratory allergens with a central hydrophobic ligand-binding cavity called a calyx. Molecules carried in the calyx by allergens are suggested to influence allergenicity, but little is known about the native ligands. Methods: To provide more information on prospective ligands, we report crystal structures, NMR, molecular dynamics, and florescence studies of a dog lipocalin allergen Can f 1 and its closely related (and cross-reactive) cat allergen Fel d 7. Results: Structural comparisons with reported lipocalins revealed that Can f 1 and Fel d 7 calyxes are open and positively charged while other dog lipocalin allergens are closed and negatively charged. We screened fatty acids as surrogate ligands, and found that Can f 1 and Fel d 7 bind multiple ligands with preferences for palmitic acid (16:0) among saturated fatty acids and oleic acid (18:1 cis-9) among unsaturated ones. NMR analysis of methyl probes reveals that conformational changes occur upon binding of pinolenic acid inside the calyx. Molecular dynamics simulation shows that the carboxylic group of fatty acids shuttles between two positively charged amino acids inside the Can f 1 and Fel d 7 calyx. Consistent with simulations, the stoichiometry of oleic acid-binding is 2:1 (fatty acid: protein) for Can f 1 and Fel d 7. Discussion: The results provide valuable insights into the determinants of selectivity and candidate ligands for pet lipocalin allergens Can f 1 and Fel d 7.
Language	English
Publishing date	2023-03-07
Publishing country	Switzerland
Document type	Journal Article
ISSN	2673-6101
ISSN (online)	2673-6101
DOI	10.3389/falgy.2023.1133412
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Relevant B cell epitopes in allergic disease.

Pomés, Anna

International archives of allergy and immunology

2009 Volume 152, Issue 1, Page(s) 1–11

Abstract: The 3-dimensional structure of an allergen defines the accessible parts on the surface of the molecule or epitopes that interact with antibodies. Mapping the antigenic determinants for IgE antibody binding has been pursued through strategies based on the ...

Abstract	The 3-dimensional structure of an allergen defines the accessible parts on the surface of the molecule or epitopes that interact with antibodies. Mapping the antigenic determinants for IgE antibody binding has been pursued through strategies based on the use of overlapping synthetic peptides, recombinant allergenic fragments or unfolded allergens. These approaches led to the identification of mostly linear epitopes and are useful for food allergens that undergo digestion or food processing. For inhaled allergens, conformational epitopes appear to be the primary targets of IgE responses. Knowledge of the molecular structure of allergens alone and in complex with antibodies that interfere with IgE antibody binding is important to understand the immune recognition of B cell-antigenic determinants on allergens and the design of recombinant allergens for immunotherapy. Starting with the molecular cloning and expression of allergens, and with the advent of X-ray crystallography and nuclear magnetic resonance techniques, we have been able to visualize conformational epitopes on allergens.
MeSH term(s)	Animals ; Aspartic Acid Endopeptidases/chemistry ; Aspartic Acid Endopeptidases/immunology ; Aspartic Acid Endopeptidases/metabolism ; Epitope Mapping ; Epitopes, B-Lymphocyte/chemistry ; Epitopes, B-Lymphocyte/immunology ; Humans ; Hypersensitivity/immunology ; Immunoglobulin Fab Fragments/chemistry ; Immunoglobulin Fab Fragments/immunology ; Immunoglobulin Fab Fragments/metabolism ; Models, Molecular
Chemical Substances	Epitopes, B-Lymphocyte ; Immunoglobulin Fab Fragments ; Aspartic Acid Endopeptidases (EC 3.4.23.-) ; allergen Bla g 2 (EC 3.4.23.-)
Language	English
Publishing date	2009-11-26
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1108932-5
ISSN	1423-0097 ; 1018-2438
ISSN (online)	1423-0097
ISSN	1018-2438
DOI	10.1159/000260078
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uh III Zs.155: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito