A molecular and in silico characterization of Hev b 4, a glycosylated latex allergen

Malik, Adeel; Arif, S.A.M.; Ahmad, Shandar; Elumalai, Sunderasan

doi:10.1016/j.ijbiomac.2007.11.004

Cited by 7 publications

(4 citation statements)

References 33 publications

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“…Ara h 1, Cor a 11, Jug r 2 and Ana o 1 allergens have been reported to contain a xylose and mannose in the N -glycan chain [50], [51]. Fucose 1,3 is reported to be present in a wide range of allergens like Hev b 1, Ara h 1, Bromelain and Papain [29], [35], [52]. The degree of mannosylation clearly differs between allergens like Der p 1, Papain, Bromelain and their structurally similar non-allergen counterparts like CPB, Calpain and Staphopain B.…”

Section: Discussionmentioning

confidence: 99%

The Glycosylation Pattern of Common Allergens: The Recognition and Uptake of Der p 1 by Epithelial and Dendritic Cells Is Carbohydrate Dependent

Al-Ghouleh¹,

Johal²,

Sharquie³

et al. 2012

PLoS ONE

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Allergens are initiators of both innate and adaptive immune responses. They are recognised at the site of entry by epithelial and dendritic cells (DCs), both of which activate innate inflammatory circuits that can collectively induce Th2 immune responses. In an attempt to have a better understanding of the role of carbohydrates in the recognition and uptake of allergens by the innate immune system, we defined common glycosylation patterns in major allergens. This was done using labelled lectins and showed that allergens like Der p 1 (Dermatophagoides pteronyssinus group 1), Fel d 1 (Felis domisticus), Ara h 1 (Arachis hypogaea), Der p 2 (Dermatophagoides pteronyssinus group 2), Bla g 2 (Blattella germanica) and Can f 1 (Canis familiaris) are glycosylated and that the main dominant sugars on these allergens are 1–2, 1–3 and 1–6 mannose. These observations are in line with recent reports implicating the mannose receptor (MR) in allergen recognition and uptake by DCs and suggesting a major link between glycosylation and allergen recognition. We then looked at TSLP (Thymic Stromal Lymphopoietin) cytokine secretion by lung epithelia upon encountering natural Der p 1 allergen. TSLP is suggested to drive DC maturation in support of allergic hypersensitivity reactions. Our data showed an increase in TSLP secretion by lung epithelia upon stimulation with natural Der p 1 which was carbohydrate dependent. The deglycosylated preparation of Der p 1 exhibited minimal uptake by DCs compared to the natural and hyperglycosylated recombinant counterparts, with the latter being taken up more readily than the other preparations. Collectively, our data indicate that carbohydrate moieties on allergens play a vital role in their recognition by innate immune cells, implicating them in downstream deleterious Th2 cell activation and IgE production.

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Section: Discussionmentioning

confidence: 99%

The Glycosylation Pattern of Common Allergens: The Recognition and Uptake of Der p 1 by Epithelial and Dendritic Cells Is Carbohydrate Dependent

Al-Ghouleh¹,

Johal²,

Sharquie³

et al. 2012

PLoS ONE

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“…N-glycans play an important role in IgE antibody binding for some allergens such as latex Heb v 4 and yellow jacket Ves m 2. For both allergens, a total reduction of IgE antibody recognition of non-glycosylated recombinant allergen versus native or allergen expressed in P. pastoris has been reported (37,38). However, the clinical relevance of CCDs is controversial (39–41).…”

Section: Discussionmentioning

confidence: 99%

Carbohydrates Contribute to the Interactions between Cockroach Allergen Bla g 2 and a Monoclonal Antibody

Gustchina

Glesner

et al. 2011

The Journal of Immunology

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The crystal structure of a murine monoclonal antibody, 4C3, that binds to the C-terminal lobe of the cockroach allergen Bla g 2, has been solved at 1.8 Å resolution. Binding of 4C3 involves different types of molecular interactions with its epitope compared to the monoclonal antibody 7C11, which binds to the N-terminal lobe of Bla g 2. We found that the 4C3 surface epitope on Bla g 2 includes a carbohydrate moiety attached to Asn268 and that a large number of antigen-antibody contacts are mediated by water molecules and ions, most likely zinc. Antibody binding experiments conducted with an enzymatically deglycosylated Bla g 2 and a N268Q mutant, showed that the carbohydrate contributes, without being essential, to the Bla g 2-4C3 mAb interaction. Inhibition of IgE antibody binding by the mAb 4C3 shows a correlation of the structurally defined epitope with reactivity with human IgE. Site-directed mutagenesis of the 4C3 mAb epitope confirmed that amino acids Lys251, Glu233, and Ile199 are important for the recognition of Bla g 2 by the 4C3 mAb antibody. The results show the relevance of X-ray crystallographic studies of allergen-antibody complexes to identify conformational epitopes that define the antigenic surface of Bla g 2.

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“…Glycol‐epitopes, which have been reported to have an important role in eliciting immune responses in humans (Aalberse ; Triguero and others ), can be affected by deglycosylation resulting in a change in the molecular mass of the protein in SDS‐PAGE and IgE‐binding ability (Stack and others ). For example, N‐glycan was found to be involved in the IgE recognition of native allergen and recombination allergen expressed in the yeast Pichia pastoris , rather than in the nonglycosylated recombinant allergen (Malik and others ; Seppala and others ). However, the IgE activity of the β‐subunit of β‐conglycinin is not influenced by deglycosylation using O‐glycosidases (Krishnan and others ).…”

Section: Introductionmentioning

confidence: 99%

Tropomyosin Contains IgE‐Binding Epitopes Sensitive to Periodate but Not to Enzymatic Deglycosylation

Ruan

Cao

Chen

et al. 2013

Journal of Food Science

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Glycosylation has been reported to affect the epitopes of food allergens, however, there are few reports on its role in crab allergen. In the present study, the effect of glycosylation on the IgE-binding activity of tropomyosin (TM), a major allergen in Scylla paramamosain, was investigated. The results showed that TM was a glycoprotein with a 0.2% carbohydrate moiety and contained O-glycan. Moreover, enzymatic deglycosylation of TM by glycosidase had no effect on the IgE-binding activity of TM. In contrast, treatment with periodate resulted in a significant reduction in its IgE-binding activity.

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A molecular and in silico characterization of Hev b 4, a glycosylated latex allergen

Cited by 7 publications

References 33 publications

The Glycosylation Pattern of Common Allergens: The Recognition and Uptake of Der p 1 by Epithelial and Dendritic Cells Is Carbohydrate Dependent

The Glycosylation Pattern of Common Allergens: The Recognition and Uptake of Der p 1 by Epithelial and Dendritic Cells Is Carbohydrate Dependent

Carbohydrates Contribute to the Interactions between Cockroach Allergen Bla g 2 and a Monoclonal Antibody

Tropomyosin Contains IgE‐Binding Epitopes Sensitive to Periodate but Not to Enzymatic Deglycosylation

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