NMR Structure and IgE Epitopes of Blo t 21, a Major Dust Mite Allergen from Blomia tropicalis

Tan, Kang Wei; Ong, Tan Ching; Gao, Yifei; Tiong, Yuen Sung; Wong, Kang Ning; Chew, Fook Tim; Mok, Yu Keung

doi:10.1074/jbc.m112.348730

Cited by 31 publications

(42 citation statements)

References 31 publications

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“…As Blo t 21 shares over 40% sequence identity with Blo t 5 (Table 2) and the structures of both proteins resemble each other (Fig. 1e, l), it has been hypothesized that Blo t 21 is a paralog of group 5 mite allergens that originated by gene duplication [79]. Despite their similarities, the allergens are not highly cross-reactive.…”

Section: Allergens Of B Tropicalismentioning

confidence: 99%

“…k Blo t 19 (2MFJ). l Blo t 21 (2LM9); the depicted residues have been shown to be a part of B-cell epitopes [79]. …”

Section: Allergens Of B Tropicalismentioning

confidence: 99%

“…The 3-D structure revealed in solution by NMR spectroscopy showed that Blo t 21 is a typical α-helical protein consisting of 3 antiparallel α-helices arranged in an elongated helical bundle (Fig. 1l) [79]. The protein contains a high percentage of surface-exposed charged residues (35.4%), with basic and acidic residues being evenly distributed.…”

Section: Allergens Of B Tropicalismentioning

confidence: 99%

“…In this way, residues Glu-74, Asp-79, Glu-84, Glu-89, and Asp-96, respectively, were shown to form distinct patches of IgE-binding residues located in opposite sides of the allergen. The Lys-107 residue has also been proposed to be involved in IgE recognition of Blo t 21 [79] (Fig. 1l).…”

Section: Allergens Of B Tropicalismentioning

confidence: 99%

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Allergens of Blomia tropicalis: An Overview of Recombinant Molecules

Silva¹,

Asam

Lackner

et al. 2017

Int Arch Allergy Immunol

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Allergic diseases are considered a major problem for healthcare systems in both developed and developing countries. House dust mites are well-known triggers of allergic manifestations. While the Dermatophagoides genus is widely distributed globally, Blomia tropicalis is the most prominent mite species in the tropical and subtropical regions of the world. Over the last decades, an increase in sensitization rates to B. tropicalis has been reported, leading to increased research efforts on Blomia allergens. In fact, 8 new allergens have been identified and characterized to different degrees. Here, we provide an overview of recent developments concerning the identification and production of recombinant Blomia allergens, as well as their structural and immunological characterization. Although considerable progress has been achieved, detailed molecule-based studies are still needed to better define the clinical relevance of Blomia allergens. Thus, the establishment of a well-standardized and fully characterized panel of allergens remains a challenge for the development of better diagnosis and therapy of allergic diseases induced by B. tropicalis.

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Section: Allergens Of B Tropicalismentioning

confidence: 99%

“…k Blo t 19 (2MFJ). l Blo t 21 (2LM9); the depicted residues have been shown to be a part of B-cell epitopes [79]. …”

Section: Allergens Of B Tropicalismentioning

confidence: 99%

Section: Allergens Of B Tropicalismentioning

confidence: 99%

Section: Allergens Of B Tropicalismentioning

confidence: 99%

See 2 more Smart Citations

Allergens of Blomia tropicalis: An Overview of Recombinant Molecules

Silva¹,

Asam

Lackner

et al. 2017

Int Arch Allergy Immunol

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show abstract

“…Gao et al (21) demonstrated that Blo t 21 was not highly cross-reactive to Blo t 5 despite a certain amount of sequence and structural identity, while Weghofer et al (22) showed that Der p 21 exhibited low IgE reactivity to Der p 5, Lep d 5 and Blo t 5 according to tests using sera from Der p 21-sensitized patients. In addition, Blo t 21 was reported to have low to moderate cross-reactivity with Blo t 5, Der p 5 and Der f 21 (24). While multiple studies have focused on Der p 5 and Blo t 5, group-5 and -21 allergens from Dermatophagoides farinae and Tyrophagus putrescentiae, which are the predominant mite species in Korea, have yet to be examined.…”

Section: Introductionmentioning

confidence: 99%

Cross-reactivity between group-5 and -21 mite allergens from Dermatophagoides farinae, Tyrophagus putrescentiae and Blomia tropicalis

Kim

Jeong

et al. 2015

Molecular Medicine Reports

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Abstract. Group-5 and group-21 allergens, produced by house dust mites and storage mites are 36.6-55.8% identical in their sequences and are recognized by at least 50% of immunoglobulin (Ig)E from the sera of individuals allergic to dust mites. In the present study, recombinant group-5 and -21 allergens from three mite species, Dermatophagoides farinae (rDer f 5 and 21), Tyrophagus putrescentiae (rTyr p 5 and 21), and Blomia tropicalis (rBlo t 5 and 21), were purified from Escherichia coli, and the IgE reactivities and cross-reactivities of these allergen variants were assessed. The IgE binding frequencies of rDer f 5, rDer f 21, rTyr p 5, rTyr p 21, rBlo t and rBlo t 21 proteins were 64. 95, 65.98, 30.41, 41.24, 30.93 and 21.65%, respectively. The IgE reactivity of rDer f 5 correlated highly with that of rDer f 21 (r=0.733). rTyr p 5 exhibited the highest level of correlation with rTyr p 21 (r=0.950), while the correlation of rBlo t 5 with rBlo t 21 was the lowest observed (r=0.104). The binding of IgE to rDer f 5 and rDer f 21 was not inhibited by any allergens but themselves. While rDer f 5 inhibited only 60.3% of IgE binding to rBlo t 5, rDer f 21 exhibited a high inhibitory effect against rTyr p 5 (93.01%), rTyr p 21 (92.12%), rBlo t 5 (86.97%) and rBlo t 21 (70.30%), implying cross-reactivity among mite species. The results of the present study demonstrated that the majority of the IgE reactivity to group-5 and -21 storage mite allergens is due to cross-reaction. It is therefore imperative to develop an accurate, component-resolved diagnosis for dust mite allergies.

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Allergen Ligands in the Initiation of Allergic Sensitization

Thomas

2014

Curr Allergy Asthma Rep

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As investigations into the innate immune responses that lead to allergic sensitization become better defined, there is a need to determine how allergens could interact with pattern recognition receptors that bind non-proteinaceous moieties. Many important allergens are not covalently bound to lipid or carbohydrate, but have structures belonging to lipid, glycan and glycolipid-binding families. These include ML-domain proteins, lipopolysaccharide-binding/cell permeability-increasing proteins, von Ebner gland lipocalins, salivary lipocalins/major urinary proteins, plant pathogenesis-related proteins PR-5 and -10, uteroglobins, non-specific lipid transfer proteins, large lipid transfer proteins and proteins with chitin and other carbohydrate-binding modules. The binding expected is overviewed with regard to importance of the allergens and their ability to elicit responses proposed from experimental models. The evidence compiled showing that allergens from the same source sensitize for different types of adaptive immune responses supports the concept that individual allergens within these sources have their own distinctive interactions with innate immunity.

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NMR Structure and IgE Epitopes of Blo t 21, a Major Dust Mite Allergen from Blomia tropicalis

Cited by 31 publications

References 31 publications

Allergens of <b><i>Blomia tropicalis</i></b>: An Overview of Recombinant Molecules

Allergens of <b><i>Blomia tropicalis</i></b>: An Overview of Recombinant Molecules

Cross-reactivity between group-5 and -21 mite allergens from Dermatophagoides farinae, Tyrophagus putrescentiae and Blomia tropicalis

Allergen Ligands in the Initiation of Allergic Sensitization

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