Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase allergen from the storage mite Acarus siro
Language English Country England, Great Britain Media electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22292590
PubMed Central
PMC3306266
DOI
10.1186/1471-2091-13-3
PII: 1471-2091-13-3
Knihovny.cz E-resources
- MeSH
- Acaridae enzymology immunology MeSH
- Allergens chemistry immunology isolation & purification MeSH
- Hypersensitivity blood immunology MeSH
- alpha-Amylases chemistry immunology isolation & purification MeSH
- Feces chemistry MeSH
- Insect Proteins chemistry immunology isolation & purification MeSH
- Immunoglobulin E blood MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Structural Homology, Protein MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Cross Reactions MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Allergens MeSH
- alpha-Amylases MeSH
- Insect Proteins MeSH
- Immunoglobulin E MeSH
BACKGROUND: Enzymatic allergens of storage mites that contaminate stored food products are poorly characterized. We describe biochemical and immunological properties of the native alpha-amylase allergen Aca s 4 from Acarus siro, a medically important storage mite. RESULTS: A. siro produced a high level of alpha-amylase activity attributed to Aca s 4. This enzyme was purified and identified by protein sequencing and LC-MS/MS analysis. Aca s 4 showed a distinct inhibition pattern and an unusual alpha-amylolytic activity with low sensitivity to activation by chloride ions. Homology modeling of Aca s 4 revealed a structural change in the chloride-binding site that may account for this activation pattern. Aca s 4 was recognized by IgE from house dust mite-sensitive patients, and potential epitopes for cross-reactivity with house dust mite group 4 allergens were found. CONCLUSIONS: We present the first protein-level characterization of a group 4 allergen from storage mites. Due to its high production and IgE reactivity, Aca s 4 is potentially relevant to allergic hypersensitivity.
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