Apyrase with anti-platelet aggregation activity from the nymph of the camel tick Hyalomma dromedarii

Apyrase is one of the essential platelet aggregation inhibitors in hematophagous arthropods due to its ability to hydrolyze ATP and ADP molecules. Here, an apyrase (TNapyrase) with antiplatelet aggregation activity was purified and characterized from the nymphs of the camel tick Hyalomma dromedarii...

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Bibliographic Details
Published in:Experimental & applied acarology 2020-03, Vol.80 (3), p.349-361
Main Authors: Masoud, Hassan M. M., Helmy, Mohamed S., Darwish, Doaa A., Abdel-Monsef, Mohamed M., Ibrahim, Mahmoud A.
Format: Article
Language:English
Subjects:
Adenosine diphosphate
Adenosine triphosphate
Agglomeration
Animal Ecology
Animal Genetics and Genomics
Animal Systematics/Taxonomy/Biogeography
Animals
Anion exchange
Anion exchanging
Antibodies
Apyrase
Apyrase - metabolism
Arthropod Proteins - metabolism
Arthropods
ATP
Binding sites
Biomedical and Life Sciences
Camelus
Columns (structural)
Entomology
Ethylenediaminetetraacetic acids
Ferric chloride
Gel electrophoresis
Gel filtration
Hyalomma dromedarii
Iron chlorides
Isoelectric focusing
Life Sciences
Nucleotides
Nymph
Platelet Aggregation
Platelets
Sodium lauryl sulfate
Ticks - enzymology
Zinc chloride
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Summary:Apyrase is one of the essential platelet aggregation inhibitors in hematophagous arthropods due to its ability to hydrolyze ATP and ADP molecules. Here, an apyrase (TNapyrase) with antiplatelet aggregation activity was purified and characterized from the nymphs of the camel tick Hyalomma dromedarii through anion exchange and gel filtration columns. The homogeneity of TNapyrase was confirmed by native-PAGE, SDS-PAGE as well as with isoelectric focusing. Purified TNapyrase had a molecular mass of 25 kDa and a monomer structure. TNapyrase hydrolyzed various nucleotides in the order of ATP > PPi > ADP > UDP > 6GP. The K m value was 1.25 mM ATP and its optimum activity reached at pH 8.4. The influence of various ions on TNapyrase activity showed that FeCl 2 , FeCl 3 and ZnCl 2 are activators of TNapyrase. EDTA inhibited TNapyrase activity competitively with a single binding site on the molecule and K i value of 2 mM. Finally, TNapyrase caused 70% inhibition of ADP-stimulated platelets aggregation and is a possible target for antibodies in future tick vaccine studies.
ISSN:0168-8162
1572-9702
DOI:10.1007/s10493-020-00471-9