Complete 1H, 13C and 15N resonance assignments of Blo t 5, a major mite allergen from Blomia tropicalis

Naik, Mandar T.; Chang, Chi‐Fon; Kuo, I-Chun; Yu, Tsunai; Fang, P.; Chua, Kee Chaing; Huang, Tai-huang

doi:10.1007/s10858-006-9113-y

Cited by 6 publications

(3 citation statements)

References 2 publications

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“…The crystal structure of Der p 5 shows a bundle of coiled coils 134 that can polymerise to create a cage with a hydrophobic cavity. The monomer structure agrees with that solved by NMR for Blo t 5 135 both of which differ in detail from that of Chan et al 136 It could be speculated that the group 5, 7 and 21 allergens might bind molecules that resemble pathogen associated microbial patterns (PAMPS) and thus compete favorable for interactions with the innate immune system and that the group 4 amylase might similarly bind to carbohydrates or glycolipids.…”

Section: Properties Of Allergenssupporting

confidence: 77%

House dust allergy and immunotherapy

Thomas

2012

Human Vaccines & Immunotherapeutics

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HDM allergy is associated with asthma, allergic rhinitis and atopic dermatitis. In many countries childhood asthma is predominantly found in HDM-allergic children with their probability of developing disease being proportional to their IgE antibody titers and the early development of Th2 responses. While the pathogenesis is complex and increasingly linked to infection the immunologically-based allergen immunotherapy and anti-IgE antibody therapy are highly beneficial. Immunotherapy could be a short-term treatment providing lifelong relief but the current regimens depend on repeated administration of allergen over years. Immunological investigations point to a contribution of responses outside the Th2 pathway and multiple potential but unproven control mechanisms. Over half of the IgE antibodies are directed to the group 1 and 2 allergens with most of remainder to the group 4, 5, 7 and 21 allergens. This hierarchy found in high and low responders provides a platform for introducing defined allergens into immunotherapy and defined reagents for investigation.

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Section: Properties Of Allergenssupporting

confidence: 77%

House dust allergy and immunotherapy

Thomas

2012

Human Vaccines & Immunotherapeutics

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“…We have employed a multifaceted approach, including analytical ultracentrifugation, small-angle X-ray scattering, gel filtration, crosslinking, and NMR, to confirm the monometric state of Blo t 5 under our experimental conditions (data not shown). Blo t 5 gave a reasonably resolved, monodispersed spectrum (colored red in Figure 2), and practically complete 1 H-, 13 C-, and 15 N-NMR resonance assignments were attained by using the triple resonance experiments (Naik et al, 2007). The structure of Blo t 5 was determined by using distance and angle restraints derived by using the solution NMR methodology and is represented as a 20 conformer ensemble in Figure 1B.…”

Section: Three-dimensional Structure Of Blo Tmentioning

confidence: 99%

Roles of Structure and Structural Dynamics in the Antibody Recognition of the Allergen Proteins: An NMR Study on Blomia tropicalis Major Allergen

et al. 2008

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Blo t 5 is the major allergen from Blomia tropicalis mites and shows strong IgE reactivity with up to 90% of asthmatic and rhinitis patients' sera. The NMR solution structure of Blo t 5 comprises three long alpha helices, forming a coiled-coil, triple-helical bundle with a left-handed twist. TROSY-NMR experiments were used to study Blo t 5 interaction with the Fab' of a specific monoclonal antibody, mAb 4A7. The mAb epitope comprises two closely spaced surfaces, I and II, connected by a sharp turn and bearing critical residues Asn46 and Lys47 on one surface, and Lys54 and Arg57 on the other. This discontinuous epitope overlaps with the human IgE epitope(s) of Blo t 5. Epitope surface II is further predicted to undergo conformational exchange in the millisecond to microsecond range. The results presented are critical for the design of a hypoallergenic Blo t 5 for efficacious immunotherapy of allergic diseases.

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“…These amide detection techniques using antibody fragments have been successfully applied to the allergen Blo t 5 in complex with a Fab. A discontinuous epitope was identified by comparing the 1 H- 15 N chemical shift perturbations of the bound and free allergen ( 135 , 136 ). This epitope was shown to overlap with binding sites of patient polyclonal IgE.…”

Section: Epitopes Defined By Nuclear Magnetic Resonance (Nmr)mentioning

confidence: 99%

Structural Aspects of the Allergen-Antibody Interaction

2020

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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.

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Complete 1H, 13C and 15N resonance assignments of Blo t 5, a major mite allergen from Blomia tropicalis

Cited by 6 publications

References 2 publications

House dust allergy and immunotherapy

House dust allergy and immunotherapy

Roles of Structure and Structural Dynamics in the Antibody Recognition of the Allergen Proteins: An NMR Study on Blomia tropicalis Major Allergen

Structural Aspects of the Allergen-Antibody Interaction

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