A naturally occurring α-amylase inhibitor (α-AI) of Triticum aestivum protects wheat grain from gramnivorous arthropod pests. The α-AI (Type-I) was incorporated into carbohydrate and protein diets to test its inhibitory activity on the stored-product mites Acarus siro, Lepidoglyphus destructor and Tyrophagus putrescentiae (Acari: Astigmata). Growth tests of mites fed the various diets were used to compare the suppressive effects. The final population size of mites attained from an initial population of 50 specimens maintained under controlled conditions (85 % relative humidity and 25 °C) was compared after 21 days of cultivation. The results showed that α-AI in the concentration in the range of 0.01-1 mg g(-1) did not suppress the growth of the tested stored-product mites. α-AI at a concentration of 10 mg g(-1) exerted a growth-suppressive effect that depended on the diet and species of the mites. The growth rate of A. siro was affected by the type of diet and was higher on carbohydrate diet than on the protein diet, the suppressive effect of α-AI was on the both diets. The growth-suppressive effect of α-AI on L. destructor and T. putrescentiae was significant when they were fed the protein diet but not when they were fed the carbohydrate diet. The higher resistance of tested mites to α-AI (proteinaceous) compared to non-proteinaceous acarbose corresponds to a powerful proteotolytic system in the mite gut. The results are discussed in terms of the adaptability of mites to utilize the starch from food sources.

• MeSH
• dieta MeSH
• druhová specificita MeSH
• rostlinné proteiny toxicita   MeSH
• roztoči účinky léků   růst a vývoj   MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• rostlinné proteiny MeSH
• WDAI-3 protein, Triticum aestivum MeSH Prohlížeč

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.

• MeSH
• Acaridae enzymologie   imunologie   MeSH
• alergeny chemie   imunologie   izolace a purifikace   MeSH
• alergie krev   imunologie   MeSH
• alfa-amylasy chemie   imunologie   izolace a purifikace   MeSH
• feces chemie   MeSH
• hmyzí proteiny chemie   imunologie   izolace a purifikace   MeSH
• imunoglobulin E krev   MeSH
• lidé MeSH
• molekulární sekvence - údaje MeSH
• sekvence aminokyselin MeSH
• sekvenční seřazení MeSH
• strukturní homologie proteinů MeSH
• terciární struktura proteinů MeSH
• vazba proteinů MeSH
• zkřížené reakce MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• alergeny MeSH
• alfa-amylasy MeSH
• hmyzí proteiny MeSH
• imunoglobulin E MeSH