Lep d 2 polymorphisms in wild and cultured <i>Lepidoglyphus destructor</i> mites

Kaiser, Liselotte; Gafvelin, Guro; Johansson, E.; Hage, Marianne van; Rasool, Omid

doi:10.1046/j.1432-1033.2003.03412.x

Cited by 7 publications

(6 citation statements)

References 28 publications

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“…The genome organization of Der f 22 was similar to that of Der f 2, in terms of the number of introns and exons. Curiously, the intron size of Der f 22 (78 bp) showed more similarity to that of Lep d 2.01 (76 bp) and Lep d 2.02 (75 bp) 19 as compared to Der f 2 (90 bp) 12 . However, the intron of the Der f 22 gene is located further downstream compared to Der f 2, Lep d 2.01 and Lep d 2.02.…”

Section: Discussionmentioning

confidence: 95%

Characterization of Der f 22 - a paralogue of the major allergen Der f 2

Reginald

Tan

Chen

et al. 2018

Sci Rep

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We previously identified an expressed sequence tag clone, Der f 22, showing 41% amino acid identity to published Der f 2, and show that both genes are possible paralogues. The objective of this study was to characterize the genomic, proteomic and immunological functions Der f 22 and Der f 2. The full-length sequence of Der f 2 and Der f 22 coded for mature proteins of 129 and 135 amino acids respectively, both containing 6 cysteine residues. Phylogenetic analysis of known group 2 allergens and their homologues from our expressed sequence tag library showed that Der f 22 is a paralogue of Der f 2. Both Der f 2 and Der f 22 were single gene products with one intron. Both allergens showed specific IgE-binding to over 40% of the atopic patients, with limited of cross-reactivity. Both allergens were detected at the gut region of D. farinae by immunostaining. Der f 22 is an important allergen with significant IgE reactivity among the atopic population, and should be considered in the diagnostic panel and evaluated as future hypoallergen vaccine therapeutic target.

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Section: Discussionmentioning

confidence: 95%

Characterization of Der f 22 - a paralogue of the major allergen Der f 2

Reginald

Tan

Chen

et al. 2018

Sci Rep

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“…The amino acid sequence diversity of individual allergens has been described in wild or cultured house dust mites (5,29,30,32,35) or storage mites (16). Small changes in the amino acid sequences of given allergens can influence their allergenicities (10).…”

mentioning

confidence: 99%

Analysis of Amino Acid Sequence Variations and Immunoglobulin E-Binding Epitopes of German Cockroach Tropomyosin

Jeong

Lee

et al. 2004

Clin Vaccine Immunol

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The allergenicities of tropomyosins from different organisms have been reported to vary. The cDNA encoding German cockroach tropomyosin (Bla g 7) was isolated, expressed, and characterized previously. In the present study, the amino acid sequence variations in German cockroach tropomyosin were analyzed in order to investigate its influence on allergenicity. We also undertook the identification of immunodominant peptides containing immunoglobulin E (IgE) epitopes which may facilitate the development of diagnostic and immunotherapeutic strategies based on the recombinant proteins. Two-dimensional gel electrophoresis and immunoblot analysis with mouse anti-recombinant German cockroach tropomyosin serum was performed to investigate the isoforms at the protein level. Reverse transcriptase PCR (RT-PCR) was applied to examine the sequence diversity. Eleven different variants of the deduced amino acid sequences were identified by RT-PCR. German cockroach tropomyosin has only minor sequence variations that did not seem to affect its allergenicity significantly. These results support the molecular basis underlying the cross-reactivities of arthropod tropomyosins. Recombinant fragments were also generated by PCR, and IgE-binding epitopes were assessed by enzyme-linked immunosorbent assay. Sera from seven patients revealed heterogeneous IgE-binding responses. This study demonstrates multiple IgE-binding epitope regions in a single molecule, suggesting that full-length tropomyosin should be used for the development of diagnostic and therapeutic reagents.

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“…However, this classification is complicated by the existence of similar structural scenarios in different structural classes.Up-and-down β -barrel: includes P80384, the major allergen Lep d 2 from Fodder mite ( Lepidoglyphus destructor ) [22], as well as other group 2 allergens from dust mite species, for example, Der f 2 (P49278) from Dermatophagoides farinae [23]. …”

Section: Resultsmentioning

confidence: 99%

“…Up-and-down β -barrel: includes P80384, the major allergen Lep d 2 from Fodder mite ( Lepidoglyphus destructor ) [22], as well as other group 2 allergens from dust mite species, for example, Der f 2 (P49278) from Dermatophagoides farinae [23]. …”

Section: Resultsmentioning

confidence: 99%

Reduction of the Number of Major Representative Allergens: From Clinical Testing to 3-Dimensional Structures

Liu

Huang

et al. 2014

Mediators of Inflammation

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Vast amounts of allergen sequence data have been accumulated, thus complicating the identification of specific allergenic proteins when performing diagnostic allergy tests and immunotherapy. This study aims to rank the importance/potency of the allergens so as to logically reduce the number of allergens and/or allergenic sources. Meta-analysis of 62 allergenic sources used for intradermal testing on 3,335 allergic patients demonstrated that in southern China, mite, sesame, spiny amaranth, Pseudomonas aeruginosa, and house dust account for 88.0% to 100% of the observed positive reactions to the 62 types of allergenic sources tested. The Kolmogorov-Smironov Test results of the website-obtained allergen data and allergen family featured peptides suggested that allergen research in laboratories worldwide has been conducted in parallel on many of the same species. The major allergens were reduced to 21 representative allergens, which were further divided into seven structural classes, each of which contains similar structural components. This study therefore has condensed numerous allergenic sources and major allergens into fewer major representative ones, thus allowing for the use of a smaller number of allergens when conducting comprehensive allergen testing and immunotherapy treatments.

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Lep d 2 polymorphisms in wild and cultured Lepidoglyphus destructor mites

Cited by 7 publications

References 28 publications

Characterization of Der f 22 - a paralogue of the major allergen Der f 2

Characterization of Der f 22 - a paralogue of the major allergen Der f 2

Analysis of Amino Acid Sequence Variations and Immunoglobulin E-Binding Epitopes of German Cockroach Tropomyosin

Reduction of the Number of Major Representative Allergens: From Clinical Testing to 3-Dimensional Structures

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