Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase allergen from the storage mite Acarus siroReportar como inadecuado

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BMC Biochemistry

, 13:3

Protein and enzyme biochemistry


BackgroundEnzymatic 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.

ResultsA. 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.

ConclusionsWe 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.

KeywordsAca s 4 Acarus siro α-amylases group 4 mite allergens storage mites AbbreviationsAca s 4a group 4 allergen from Acarus siro

Der p 4 and Der f 4a group 4 allergen from Dermatophagoides pteronyssinus and D. farinae, respectively

PPA and HPAporcine and human pancreatic α-amylase, respectively

RBB-StarchRemazol Brilliant Blue dyed starch

PAMIpeptide α-amylase inhibitor

WI-1 and WI-3wheat α-amylase inhibitors 1 and 3, respectively

αAI-1bean α-amylase inhibitor 1


Electronic supplementary materialThe online version of this article doi:10.1186-1471-2091-13-3 contains supplementary material, which is available to authorized users.

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Autor: Jana Pytelková - Martin Lepšík - Miloslav Šanda - Pavel Talacko - Lucie Marešová - Michael Mareš

Fuente: https://link.springer.com/article/10.1186/1471-2091-13-3

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