Characterization of glutathione S‐transferase from dust mite, Der p 8 and its immunoglobulin E cross‐reactivity with cockroach glutathione S‐transferase

Huang, Chiung‐Hui; Liew, Lee Mei; Mah, Ka Weng; Kuo, I-Chun; Lee, B. W.; Chua, Kee Chaing

doi:10.1111/j.1365-2222.2006.02447.x

Cited by 47 publications

(52 citation statements)

References 39 publications

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“…For example, tropomyosin, a group-10 allergen, is a well-known pan-allergen that causes cross-reactivity among mites, a variety of invertebrates (5,6) including shrimps and crabs, and parasites, including Anisakis nematodes and roundworms (7)(8)(9). Group-8 mite allergens (glutathione S-transferase) have also been shown to be cross-reactive with other arthropod allergens (10,11). The group-2 allergens are cross-reactive among mite species (12,13) and are the primary allergens responsible for the cross-reactivity between HDM and SM in Korea (14).…”

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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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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“…[116][117][118][119][120][121][122][123][124][125][126][127][128] We have demonstrated that helminth infection can be associated with increased IgE responses to many different allergens, especially those structurally related to parasite antigens. 116 Individuals infected with filarial parasites were shown to have higher levels of IgE against HDM and cockroach extracts (that have several major allergens with homologues in filarial parasites) but not against timothy grass extract, an allergen extract with just a few minor allergen homologues in helminths.…”

Section: -89mentioning

confidence: 99%

“…118 Similarly, IgE binding to several Ascaris allergens can also be inhibited by Dermatophagoides pteronyssinus (Der p) or Blomia tropicalis (Blo t) extracts, including glutathione-S-transferase (GST). 120 GSTs are major allergens of HDM, 119 cockroach, 135 mold, 136,137 and parasites. 138,139 Among the 13 classes of canonical GSTs, there are many that show very little amino acid conservation.…”

Section: -89mentioning

confidence: 99%

Human Helminths and Allergic Disease: The Hygiene Hypothesis and Beyond

Santiago

Nutman

2016

The American Society of Tropical Medicine and Hygiene

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Abstract. There is much debate about the interaction between helminths and allergic disease. The "Hygiene Hypothesis," a very popular concept among scientists and the lay public, states that infections, especially during childhood, can protect against allergic diseases. Indeed, helminth infections are known to induce regulatory responses in the host that can help the control of inflammation (including allergic inflammation). However, these infections also induce type-2-associated immune responses including helminth-specific IgE that can cross-react against environmental allergens and mediate IgE-driven effector responses. Thus, it is the delicate balance between the parasites' anti-and pro-allergenic effects that define the helminth/allergy interface.The immune system has evolved, in large part, through its interaction with microbes and parasites, an interaction that drives specific or specialized immune responses to deal with the widely varying groups of microorganisms. For example, parasite-derived induction of interleukin (IL)-4, IL-5, and IL-13 coordinate the prototypical responses to metazoan helminth pathogens, 1 whereas viral-and bacterial-specific induction of Type 1 and Type 2 interferons are required for control of these types of infections.

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“…These allergens have been found at a high frequency among allergic subjects, but their titers of IgE reactivity were low (9). The mite GST has been demonstrated to be a cross-reactive allergen in D. pteronyssinus and cockroach GST, which suggests that it is a panallergen (9). GST has also been shown as an allergen in Blatella germanica (Bla g 5), arthropods, and fungi (10,11,12).…”

mentioning

confidence: 99%

“…Native and recombinant GSTs have been purified from D. pteronyssinus and are known as Der p 8. These allergens have been found at a high frequency among allergic subjects, but their titers of IgE reactivity were low (9). The mite GST has been demonstrated to be a cross-reactive allergen in D. pteronyssinus and cockroach GST, which suggests that it is a panallergen (9).…”

mentioning

confidence: 99%

Identification of Allergenic Component Tyr p 8 from Tyrophagus putrescentiae and Cross-Reactivity with Der p 8

Liao

Lin

Chiu

et al. 2013

Clin Vaccine Immunol

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Group 8 mite allergens exhibit sequence homology to glutathione S-transferases (GSTs), such as that from Dermatophagoides pteronyssinus (Der p 8). GSTs have been identified as important allergens in studies of allergens from house dust mites, cockroaches, and fungi. Our objective was to purify the native group 8 allergen from Tyrophagus putrescentiae (nTyr p 8) and generate recombinant Tyr p 8 (rTyr p 8) for immunological characterization. The allergenicity was determined by antibody recognition, IgE inhibition, and triggering of the basophil-sensitized release of histamine, using T. putrescentiae hypersensitivity sera. The results showed that the mRNA transcript of nTyr p 8 is 657 bp long, contains 218 amino acids with a molecular mass of 26 kDa, and exhibits 83% sequence homology to Der p 8. Serum samples from the allergic patients with an IgE-positive response to T. putrescentiae were analyzed to determine their IgE response to rTyr p 8. The results showed that the sera of 48 subjects (45.3%) had specific IgE against rTyr p 8. However, sera of only 19 subjects (17.9%) had specific IgE against rTyr p 8 after D. pteronyssinus absorption. Histamine release was observed from T. putrescentiae-allergic subjects in the presence of rTyr p 8. Both the nTyr p 8 and T. putrescentiae crude extract had been demonstrated to possess GST enzymatic activity. Although the specific binding of serum IgE to rTyr p 8 was only 17.9%, which indicates that rTyr p 8 was not a major allergen, the positive response to rTyr p 8 was due to the cross-reactivity with Der p 8. The group 8 mite allergen might be of use in the design of a suitable allergen for diagnosis and for the development of novel immunotherapies.

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Characterization of glutathione S‐transferase from dust mite, Der p 8 and its immunoglobulin E cross‐reactivity with cockroach glutathione S‐transferase

Abstract: A high frequency of sensitization to mite GST among allergic subjects was observed but the titres of IgE reactivity were low. The IgE cross-reactivity between mite and cockroach GST suggests that GST is a panallergen.

Cited by 47 publications

References 39 publications

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

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

Human Helminths and Allergic Disease: The Hygiene Hypothesis and Beyond

Identification of Allergenic Component Tyr p 8 from Tyrophagus putrescentiae and Cross-Reactivity with Der p 8

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