Selection and Characterization of Monoclonal Antibodies against a Major Allergen in &lt;i&gt;Dermatophagoides&lt;/i&gt;&lt;i&gt;pteronyssinus&lt;/i&gt;

Horn, Nina; Lind, Peter

doi:10.1159/000234376

Cited by 20 publications

(11 citation statements)

References 7 publications

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“…In particular, antigenic determinants on the Der I al lergens have been analyzed in detail with the use of several series of monoclonal antibodies [28][29][30], and sensitive immunoassays developed for measuring the Der I allergens [31][32][33] have made it much easier to evaluate dust mite allergen levels in houses [34,35]. However, the Der II allergens seems to have been less investigated than the Der I allergens, because they have only been purified in relatively small quantities.…”

Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Physicochemical and Immunochemical Properties of the Two Major Allergens from Dermatophagoides pteronyssinus and the Corresponding Allergens from Dermatophagoides farinae

Yasueda¹,

Mita²,

Yui³

et al. 1989

Int Arch Allergy Immunol

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Two major allergens, DPI (Der p I) and DP2 (Der p II), were isolated from the whole culture extract of Dermatophagoides pteronyssinus, and the physicochemical and immunochemical properties of these allergens were compared with those of the corresponding allergens from Dermatophagoides farinae, DF1 (Der f I)and DF2 (Der f II).On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, polyacrylamide gel isoelectric focusing and amino acid analysis, both DP1 and DP2 were demonstrated to have close physicochemical similarity with DF1 and DF2, respectively. On immunodiffusion with the use of rabbit antisera, the two Der I allergens showed the reaction of typical partial identity, while the two Der II allergens showed the reaction of almost complete identity. Radioallergosorbent test (RAST) and RAST absorption experiments with the use of sera from mite-allergic patients showed that human IgE antibody response to the Der I allergens was directed against both cross-reactive and species-specific determinants. In contrast, IgE antibodies to the Der II allergens were demonstrated to react almost completely to cross-reactive determinants.

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Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Physicochemical and Immunochemical Properties of the Two Major Allergens from Dermatophagoides pteronyssinus and the Corresponding Allergens from Dermatophagoides farinae

Yasueda¹,

Mita²,

Yui³

et al. 1989

Int Arch Allergy Immunol

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“…Other surface areas, on the other hand, are conserved between species or the substitutions may be sufficiently conservative to allow binding of cross-reactive Abs. This explains the observation that some Abs cross-react between the group 1 allergens from different species, whereas others do not (6,7).…”

Section: The Effect Of Species Variation On the Possible Ab Binding Smentioning

confidence: 99%

“…Because the house dust mites are taxonomically related, the different species contain homologous allergens with structural similarities, which causes IgE cross-reactivity (5). Patients sensitized to one species therefore often also react to the other species (6,7).…”

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confidence: 99%

The Crystal Structure of Recombinant proDer p 1, a Major House Dust Mite Proteolytic Allergen

Meno

Thorsted

Ipsen

et al. 2005

The Journal of Immunology

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Allergy to house dust mite is among the most prevalent allergic diseases worldwide. Most house dust mite allergic patients react to Der p 1 from Dermatophagoides pteronyssinus, which is a cysteine protease. To avoid heterogeneity in the sample used for crystallization, a modified recombinant molecule was produced. The sequence of the proDer p 1 allergen was modified to reduce glycosylation and to abolish enzymatic activity. The resulting rproDer p 1 preparation was homogenous and stable and yielded crystals diffracting to a resolution of 1.61 Å. The active site is located in a large cleft on the surface of the molecule. The 80-aa pro-peptide adopts a unique fold that interacts with the active site cleft and a substantial adjacent area on the mature region, excluding access to the cleft and the active site. Studies performed using crossed-line immunoelectrophoresis and IgE inhibition experiments indicated that several epitopes are covered by the pro-peptide and that the epitopes on the recombinant mature molecule are indistinguishable from those on the natural one. The structure confirms previous results suggesting a preference for aliphatic residues in the important P2 position in substrates. Sequence variations in related species are concentrated on the surface, which explains the existence of cross-reacting and species-specific antibodies. This study describes the first crystal structure of one of the clinically most important house dust mite allergens, the cysteine protease Der p 1.

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“…Other mite allergens have also been identified, but their allergenic importance remains to be established (35). Several laboratories have produced murine monoclonal antibodies (Mabs) to the Group I and Group II allergens (5,36,37). These Mabs have been used for allergen purification, epitope mapping studies, and to develop specific immunoassays for allergen quantification (37).…”

Section: Identification and Standardizationmentioning

confidence: 99%

Dust mite allergens and asthma—A worldwide problem

Platts‐Mills¹,

deWeck²,

Aalberse³

et al. 1989

Journal of Allergy and Clinical Immunology

599

304

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After the discovery ofhouse dust mites in 1964 their association with asthma has been reported from many different parts of the world including the developing countries. Two sets of major allergens from mites of the genus Dermatophagoides are now well recognized. The Group I allergens are glycoproteins of relative molecular mass (Mr) 25 000, which show both structural homology and cross-reactivity. The allergen Der p I has been cloned and sequenced confirming the M, and establishing its nature as a protease. The Group II allergens (Mr 15 000) show even closer homology and cross-reactivity.Specific immunoassays for Group I and Group II allergens, using monospecific antisera and monoclonal antibodies, have been standardized and are suitable for measuring allergen levels in different parts of the world.Measures for reducing the levels of mite allergens in houses include the covering of mattresses, hot washing of bedding, and removal of carpets from bedrooms as well as humidity control, vacuum cleaning, and the use ofacaricides in the rest ofthe house. There is already evidence that these procedures can cause a major improvement in the symptoms of asthma. While provisional standards for both sensitization to mites and also mite allergen exposure can now be recommended, there is an urgent needfor controlled studies using protocols demonstrated to reduce mite allergen levels by at least tenfold and for further international collaboration.

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Selection and Characterization of Monoclonal Antibodies against a Major Allergen in <i>Dermatophagoides</i><i>pteronyssinus</i>

Cited by 20 publications

References 7 publications

Comparative Analysis of Physicochemical and Immunochemical Properties of the Two Major Allergens from <i>Dermatophagoides pteronyssinus </i>and the Corresponding Allergens from <i>Dermatophagoides farinae</i>

Comparative Analysis of Physicochemical and Immunochemical Properties of the Two Major Allergens from <i>Dermatophagoides pteronyssinus </i>and the Corresponding Allergens from <i>Dermatophagoides farinae</i>

The Crystal Structure of Recombinant proDer p 1, a Major House Dust Mite Proteolytic Allergen

Dust mite allergens and asthma—A worldwide problem

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