Dust Mite

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W R Thomas - One of the best experts on this subject based on the ideXlab platform.

  • house Dust Mite allergens in asthma and allergy
    Trends in Molecular Medicine, 2010
    Co-Authors: W R Thomas, Belinda J Hales, Wendyanne Smith
    Abstract:

    IgE antibodies in house Dust Mite (HDM) allergy follow a predictable pattern. Half are directed against two dominant allergens and the remainder largely against four midpotency allergens. This hierarchical pattern is not changed by the titre of the IgE response or severity of disease. The structures of these allergens are known and they can be produced as authentic recombinant allergens. There is also evidence that the allergenicity is augmented by the biological activity of the key allergens, validating them as targets for vaccination. Collectively, these developments should facilitate the development of new diagnostics, improve immunotherapy and allow vaccination with defined reagents. Highly purified recombinant polypeptides representing the important Mite allergens are now available so that informative and reproducible experiments can be performed with Mite allergens in place of poorly defined and variable extracts.

  • characterization and immunobiology of house Dust Mite allergens
    International Archives of Allergy and Immunology, 2002
    Co-Authors: W R Thomas, Belinda J Hales, Wendyanne Smith, Kristina L Mills, Richard M Obrien
    Abstract:

    The examination of house Dust Mite extracts has indicated that over 30 different proteins can induce IgE antibody in patients allergic to the house Dust Mite. There are however dominant specificities especially the group 1 and 2 allergens which can account for much of the allergenicity of extracts. Of the 19 denominated allergens, the major IgE binding has been reported for the group 1, 2, 3, 9, 11, 14 and 15 allergens. The high-molecular-weight group 11, 14 and 15 allergens have only recently been described and although high IgE binding has been anticipated from immunoblotting, there is a need for considerable corroboration. Similarly, the study of the group 3 and 9 serine protease allergens has been incomplete. The group 4, 5, 7 and 8 allergens have shown intermediate IgE binding and the group 10 tropomyosins are of interest because of their potential cross-reactivity with allergen from disparate species. Although the progress with the production of recombinant group 1 allergens has been recent, many of the allergens can be produced as high IgE-binding polypeptides. The tertiary structure of the group 2 allergens has been determined from recombinant proteins and they are an excellent model for the investigation of modified allergens. An unexpected property of the group 1, 2 and 3 allergens has been the high degree of polymorphism found by cDNA analysis. It has however been possible to identify sequences to represent the variation in the natural allergens. The group 7 and 14 allergens show secondary modifications which vary in different extracts creating batch variation. While some estimate of the importance of allergens can be obtained from IgE binding, few analyses of T-cell responses have been made and these regulate both the development of, and the protection from sensitization.

  • molecular analysis of the group 1 and 2 allergens from the house Dust Mite euroglyphus maynei
    International Archives of Allergy and Immunology, 1999
    Co-Authors: Wendyanne Smith, B.j. Hart, Kristina L Mills, L A Hazell, W R Thomas
    Abstract:

    Background: There is increasing evidence that the house Dust Mite Euroglyphus maynei may be a significant source of allergic sensitization. The structural information for the E. may

Alain Jacquet - One of the best experts on this subject based on the ideXlab platform.

  • the role of innate immunity activation in house Dust Mite allergy
    Trends in Molecular Medicine, 2011
    Co-Authors: Alain Jacquet
    Abstract:

    House Dust Mite (HDM) allergy is a frequent inflammatory disease found worldwide. Although allergen-specific CD4 + Th2 cells orchestrate the HDM allergic response, notably through induction of IgE directed towards Mite allergens, recent studies have demonstrated that innate immunity activation also plays a critical role in HDM-induced allergy pathogenesis. HDM allergens can not only be considered proteins that induce adaptive Th2-biased responses in susceptible subjects but also as strong activators of innate immune cells, including skin keratinocytes and airway epithelial cells. The contribution of microbial adjuvant factors, derived from HDM carriers or the environment, is also essential in such cell stimulation. This review highlights how HDM allergens, together with microbial compounds, promote allergic responses through pattern recognition receptor-dependent pathways.

  • vaccination with the recombinant allergen proder p 1 complexed with the cationic lipid dic14 amidine prevents allergic responses to house Dust Mite
    Molecular Therapy, 2005
    Co-Authors: Alain Jacquet, Jeanfrancois Vanderschrick, Abdelatif Elouahabi, Mauro Magi, Lida Garcia, Michel Vandenbranden, Jean Marie Ruysschaert
    Abstract:

    Abstract The present study evaluated the prophylactic potential of ProDer p 1, the recombinant precursor form of the major Mite allergen Der p 1, combined with the cationic lipid diC14-amidine in a murine model of house Dust Mite allergy. Naive mice vaccinated with the amidine/allergen complex developed a Th1-biased immune response characterized by the absence of specific IgE, the production of specific IgG2a, and the presence of IFN-γ in splenocyte cultures. In contrast, ProDer p 1 adjuvanted with alum induced typical strictly Th2-biased allergic responses with strong IgG1 and IgE titers and IL-5 secretion. Removal of negatively charged sialic acids in ProDer p 1 or increasing the ionic strength reduced the binding of ProDer p 1 to the cationic liposomes and resulted in a decrease of the allergen immunogenicity, suggesting that complexation is required for triggering an optimal immune response. Finally, prophylactic vaccination with ProDer p 1–diC14-amidine reduced drastically the production of specific IgE and airway eosinophilia following subsequent immunization with Der p 1–alum and challenge with aerosolized house Dust Mite extracts. In conclusion, recombinant ProDer p 1 complexed with diC14-amidine could represent an efficient prophylactic vaccine against house Dust Mite allergy.

  • high level expression of recombinant house Dust Mite allergen der p 1 in pichia pastoris
    Clinical & Experimental Allergy, 2002
    Co-Authors: Alain Jacquet, Mauro Magi, H Petry, Alex Bollen
    Abstract:

    BACKGROUND: The major house Dust Mite Der p 1 allergen is associated with allergic disease. Heterologous over-expression of biologically active Der p 1 was previously attempted but with liMited success. OBJECTIVE: The aim of this study was to establish an efficient system for the production of recombinant Der p 1. METHODS: The proform of Der p 1 was expressed in Pichia pastoris as a fusion with the alpha mating factor signal sequence. The recombinant product was purified from culture medium and compared to Der p 1 isolated from Mite culture, in terms of enzymatic activity as well as IgE binding capacity. RESULTS: ProDer p 1 was efficiently secreted into culture medium as a hyperglycosylated protein of 40-60 kDa. Postpurification dialysis in acidic buffer was required for the autocatalytic processing of Der p 1. During this treatment, the prosequence was efficiently removed to give highly glycosylated recombinant mature Der p 1. Competition ELISA experiments as well as cysteine proteinase activity assays indicated that recombinant processed Der p 1 was similar to natural Der p 1 isolated from Mite cultures in terms of IgE binding and enzymatic activities. However, the histamine releasing activity of recombinant Der p 1 was slightly weaker than that of natural Der p 1. CONCLUSION: This efficient system for recombinant Der p 1 expression leads the way for the design of new diagnostics for house Dust Mite allergy, epitope mapping, allergen engineering, structural and immunological studies and new immunotherapeutic treatments.

  • high level expression in mammalian cells of recombinant house Dust Mite allergen proder p 1 with optimized codon usage
    International Archives of Allergy and Immunology, 2001
    Co-Authors: Marc Massaer, Mauro Magi, Alex Bollen, Pasqualina Mazzu, Michele Haumont, Veronique Daminet, Alain Jacquet
    Abstract:

    Background: The major house Dust Mite allergen Der p 1 is associated with allergic diseases such as asthma. Production of recombinant Der p 1 was previously attempted, but with limi

Johannes C Van Der Wouden - One of the best experts on this subject based on the ideXlab platform.

  • sublingual immunotherapy not effective in house Dust Mite allergic children in primary care
    Pediatric Allergy and Immunology, 2012
    Co-Authors: Cindy M A De Bot, Heleen Moed, Esther Roder, Marjolein Y. Berger, Hans De Groot, Johan C De Jongste, Wim C J Hop, Roy Gerth Van Wijk, Patrick J E Bindels, Johannes C Van Der Wouden
    Abstract:

    Background: Sublingual immunotherapy (SLIT) as a therapy for the treatment of allergic rhinitis in children might be acceptable as an alternative for subcutaneous immunotherapy. However, the efficacy of SLIT with house Dust Mite extract is not well established. Objective: To investigate whether SLIT in house Dust Mite–allergic children recruited in primary care is effective and safe. Methods: Children aged 6–18 years (n = 251) recruited in primary care with a house Dust Mite–induced allergic rhinitis received either SLIT or placebo for 2 years. Symptoms and medication use were assessed throughout the study. Primary outcome parameter was the mean total nose symptom score (scales 0–12) during the autumn of the second treatment year. Safety was assessed by recording any adverse event. Results: Overall, the mean nose symptom score ± s.d. after 2 years of treatment showed no significant effect of SLIT (symptom score intervention group 2.26 ± 1.84 vs. placebo group, 2.02 ± 1.67; p = 0.08). There were no significant differences in secondary outcomes, nor in subgroup analyses. The number of patients reporting adverse events was comparable between both groups. Conclusions: Sublingual immunotherapy with house Dust Mite allergen was not better than placebo in reducing rhinitis symptoms in house Dust Mite–allergic children in primary care. SLIT as administered in this study can be considered safe.

  • randomized double blind placebo controlled trial of sublingual immunotherapy in children with house Dust Mite allergy in primary care study design and recruitment
    BMC Family Practice, 2008
    Co-Authors: Cindy M A De Bot, Heleen Moed, Esther Roder, Marjolein Y. Berger, Hans De Groot, Johan C De Jongste, Roy Gerth Van Wijk, Johannes C Van Der Wouden
    Abstract:

    For respiratory allergic disorders in children, sublingual immunotherapy has been developed as an alternative to subcutaneous immunotherapy. Sublingual immunotherapy is more convenient, has a good safety profile and might be an attractive option for use in primary care. A randomized double-blind placebo-controlled study was designed to establish the efficacy of sublingual immunotherapy with house Dust Mite allergen compared to placebo treatment in 6 to18-year-old children with allergic rhinitis and a proven house Dust Mite allergy in primary care. Described here are the methodology, recruitment phases, and main characteristics of the recruited children. Recruitment took place in September to December of 2005 and 2006. General practitioners (in south-west Netherlands) selected children who had ever been diagnosed with allergic rhinitis. Children and parents could respond to a postal invitation. Children who responded positively were screened by telephone using a nasal symptom score. After this screening, an inclusion visit took place during which a blood sample was taken for the RAST test. A total of 226 general practitioners invited almost 6000 children: of these, 51% was male and 40% <12 years of age. The target sample size was 256 children; 251 patients were finally included. The most frequent reasons given for not participating were: absence or mildness of symptoms, absence of house Dust Mite allergy, and being allergic to grass pollen or tree pollen only. Asthma symptoms were reported by 37% of the children. Of the enrolled children, 71% was sensitized to both house Dust Mite and grass pollen. Roughly similar proportions of children were diagnosed as being sensitized to one, two, three or four common inhalant allergens. Our study was designed in accordance with recent recommendations for research on establishing the efficacy of sublingual immunotherapy; 98% of the target sample size was achieved. This study is expected to provide useful information on sublingual immunotherapy with house Dust Mite allergen in primary care. The results on efficacy and safety are expected to be available by 2010. the trial is registered as ISRCTN91141483 (Dutch Trial Register)

B.j. Hart - One of the best experts on this subject based on the ideXlab platform.

  • molecular analysis of the group 1 and 2 allergens from the house Dust Mite euroglyphus maynei
    International Archives of Allergy and Immunology, 1999
    Co-Authors: Wendyanne Smith, B.j. Hart, Kristina L Mills, L A Hazell, W R Thomas
    Abstract:

    Background: There is increasing evidence that the house Dust Mite Euroglyphus maynei may be a significant source of allergic sensitization. The structural information for the E. may

  • molecular characterisation of group i allergen eur m i from house Dust Mite euroglyphus maynei
    International Archives of Allergy and Immunology, 1992
    Co-Authors: N A Kent, Michael Hill, J N Keen, Peter W H Holland, B.j. Hart
    Abstract:

    Using the polymerase chain reaction (PCR) we have amplified and cloned genomic DNA encoding the secreted group I allergen proteins from the house Dust Mite species Euroglyphus maynei, Dermatophagoides pteronyssinus and D. farinae. Affinity chromatography using a monoclonal antibody to the allergen Der p I was used to purify the group I protein from E. maynei. We present the deduced amino acid sequence of a new member of the group I house Dust Mite allergen family Eur m I. The three proteins show a high level of primary structure similarity: Eur m I and Der p I show 85% amino acid identity, and the three allergen amino acid sequences taken together show 78% identity. A potential N-glycosylation site and residues of the cysteine protease active site are also conserved between the three proteins.

Wendyanne Smith - One of the best experts on this subject based on the ideXlab platform.

  • house Dust Mite allergens in asthma and allergy
    Trends in Molecular Medicine, 2010
    Co-Authors: W R Thomas, Belinda J Hales, Wendyanne Smith
    Abstract:

    IgE antibodies in house Dust Mite (HDM) allergy follow a predictable pattern. Half are directed against two dominant allergens and the remainder largely against four midpotency allergens. This hierarchical pattern is not changed by the titre of the IgE response or severity of disease. The structures of these allergens are known and they can be produced as authentic recombinant allergens. There is also evidence that the allergenicity is augmented by the biological activity of the key allergens, validating them as targets for vaccination. Collectively, these developments should facilitate the development of new diagnostics, improve immunotherapy and allow vaccination with defined reagents. Highly purified recombinant polypeptides representing the important Mite allergens are now available so that informative and reproducible experiments can be performed with Mite allergens in place of poorly defined and variable extracts.

  • characterization and immunobiology of house Dust Mite allergens
    International Archives of Allergy and Immunology, 2002
    Co-Authors: W R Thomas, Belinda J Hales, Wendyanne Smith, Kristina L Mills, Richard M Obrien
    Abstract:

    The examination of house Dust Mite extracts has indicated that over 30 different proteins can induce IgE antibody in patients allergic to the house Dust Mite. There are however dominant specificities especially the group 1 and 2 allergens which can account for much of the allergenicity of extracts. Of the 19 denominated allergens, the major IgE binding has been reported for the group 1, 2, 3, 9, 11, 14 and 15 allergens. The high-molecular-weight group 11, 14 and 15 allergens have only recently been described and although high IgE binding has been anticipated from immunoblotting, there is a need for considerable corroboration. Similarly, the study of the group 3 and 9 serine protease allergens has been incomplete. The group 4, 5, 7 and 8 allergens have shown intermediate IgE binding and the group 10 tropomyosins are of interest because of their potential cross-reactivity with allergen from disparate species. Although the progress with the production of recombinant group 1 allergens has been recent, many of the allergens can be produced as high IgE-binding polypeptides. The tertiary structure of the group 2 allergens has been determined from recombinant proteins and they are an excellent model for the investigation of modified allergens. An unexpected property of the group 1, 2 and 3 allergens has been the high degree of polymorphism found by cDNA analysis. It has however been possible to identify sequences to represent the variation in the natural allergens. The group 7 and 14 allergens show secondary modifications which vary in different extracts creating batch variation. While some estimate of the importance of allergens can be obtained from IgE binding, few analyses of T-cell responses have been made and these regulate both the development of, and the protection from sensitization.

  • molecular analysis of the group 1 and 2 allergens from the house Dust Mite euroglyphus maynei
    International Archives of Allergy and Immunology, 1999
    Co-Authors: Wendyanne Smith, B.j. Hart, Kristina L Mills, L A Hazell, W R Thomas
    Abstract:

    Background: There is increasing evidence that the house Dust Mite Euroglyphus maynei may be a significant source of allergic sensitization. The structural information for the E. may