On the potential significance of the enzymatic activity of mite allergens to immunogenicity. Clues to structure and function revealed by molecular characterization

Robinson, Clive; Kalsheker, Noor; Srinivasan, Narayanaswamy; King, Charles M.; Garrod, David R.; Thompson, Philip J.; Stewart, Geoffrey A.

doi:10.1111/j.1365-2222.1997.tb00667.x

Cited by 108 publications

(101 citation statements)

References 49 publications

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“…In addition, Tyr-372 (Fig. 3a, red) of factor XIII, neighboring the catalytic triad (orange), corresponds to the tyrosine that has been recognized as unique to the mite allergen cysteine proteases (8). The fact that Der f 2 inhibited guinea pig liver transglutaminase 2 is also interesting as it relates to the structural similarity described above.…”

Section: Resultsmentioning

confidence: 90%

“…However, there have been no clues for their functions except for their expression patterns. This is in contrast to the case of the other major allergen group including Der f 1 and Der p 1, because they were found to be cysteine proteases, and their activity was suggested to be involved in the induction of allergic responses (8). Therefore, the innate functions of Der f 2 and Der p 2 have interested many allergy researchers.…”

mentioning

confidence: 98%

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Solution Structure of Der f 2, the Major Mite Allergen for Atopic Diseases

Ichikawa¹,

Hatanaka²,

Yuuki³

et al. 1998

Journal of Biological Chemistry

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House dust mites cause heavy atopic diseases such as asthma and dermatitis. Among allergens from Dermatophagoides farinae, Der f 2 shows the highest positive rate for atopic patients, but its biological function in mites has been perfectly unknown, as well as the functions of its homologs in human and other animals. We have determined the tertiary structure of Der f 2 by multidimensional nuclear magnetic resonance spectroscopy. Der f 2 was found to be a single-domain protein of immunoglobulin fold, and its structure was the most similar to those of the two regulatory domains of transglutaminase. This fact, binding to the bacterial surface, and other small pieces of information hinted that Der f 2 is related to the innate antibacterial defense system in mites. The immunoglobulin E epitopes are also discussed on the basis of the tertiary structure.

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Section: Resultsmentioning

confidence: 90%

mentioning

confidence: 98%

Solution Structure of Der f 2, the Major Mite Allergen for Atopic Diseases

Ichikawa¹,

Hatanaka²,

Yuuki³

et al. 1998

Journal of Biological Chemistry

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show abstract

“…That Der p 1 is a proteinase has been indicated previously (6,21,24,(36)(37)(38)(39)(40)(41)(42). We reasoned that its proteolytic effects in airway epithelium might be significant to sensitization because of the degree to which airway mucosal barrier is exposed to foreign proteins.…”

Section: Discussionmentioning

confidence: 99%

Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions

Wan

Winton²,

Soeller³

et al. 1999

J. Clin. Invest.

678

528

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“…However, even high quality extracts may contain allergens to which subjects are not sensitized and may also contain proteolytic enzymes. Proteolytic enzymes can affect the stability of allergens and result in inflammatory responses in subjects [9,10]. Commercially-available cockroach extracts are particularly inconsistent in relative potency and Bla g 2 levels [11].…”

Section: Introductionmentioning

confidence: 99%

Reactivity of German Cockroach Allergen, Bla g 2, Peptide Fragments to IgE Antibodies in Patients' Sera

et al. 2008

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Bla g 2 is a cockroach allergen of great importance. This study was conducted to identify IgE-binding epitope(s) of Bla g 2 using the recombinant protein technique. Approximately 50% of tested sera showed IgE reactivity to Pichiaexpressed Bla g 2 (PrBla g 2) and E. coli-expressed Bla g 2 (ErBla g 2). Only 5.3% of serum samples showed stronger reactivity to PrBla g 2 than ErBla g 2, indicating that serum was reactive to conformational or carbohydrate epitopes. The full-length and 5 peptide fragments of Bla g 2 were produced in E. coli. All fragments showed IgE-binding activity to the cockroach-allergy patients' sera. Specifically, peptide fragments of amino acid residue 1-75 and 146-225 appeared to be important for IgE-binding. The information about the IgE-binding epitope of Bla g 2 can aid in the diagnosis and treatment for cockroach allergies.

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On the potential significance of the enzymatic activity of mite allergens to immunogenicity. Clues to structure and function revealed by molecular characterization

Cited by 108 publications

References 49 publications

Solution Structure of Der f 2, the Major Mite Allergen for Atopic Diseases

Solution Structure of Der f 2, the Major Mite Allergen for Atopic Diseases

Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions

Reactivity of German Cockroach Allergen, Bla g 2, Peptide Fragments to IgE Antibodies in Patients' Sera

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