Rdromaserpin: A novel anti-hemostatic serpin, from the Salivary glands of the hard tick hyalomma dromedarii
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F21%3A00551709" target="_blank" >RIV/60077344:_____/21:00551709 - isvavai.cz</a>
Result on the web
<a href="https://www.mdpi.com/2072-6651/13/12/913" target="_blank" >https://www.mdpi.com/2072-6651/13/12/913</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/toxins13120913" target="_blank" >10.3390/toxins13120913</a>
Alternative languages
Result language
angličtina
Original language name
Rdromaserpin: A novel anti-hemostatic serpin, from the Salivary glands of the hard tick hyalomma dromedarii
Original language description
Hemostatic disorders are caused either by platelet-related dysfunctions, defective blood coagulation, or by a combination of both, leading to an increased susceptibility to cardiovascular diseases (CVD) and other related illnesses. The unique specificity of anticoagulants from hematophagous arthropods, such as ticks, suggests that tick saliva holds great promise for discovering new treatments for these life-threatening diseases. In this study, we combined in silico and in vitro analyses to characterize the first recombinant serpin, herein called Dromaserpin, from the sialotranscriptome of the Hyalomma dromedarii tick. Our in silico data described Dromaserpin as a secreted protein of ~43 kDa with high similarities to previously characterized inhibitory serpins. The recombinant protein (rDromaserpin) was obtained as a well-structured monomer, which was tested using global blood coagulation and platelet aggregation assays. With this approach, we confirmed rDromaserpin anticoagulant activity as it significantly delayed plasma clotting in activated partial thromboplastin time and thrombin time assays. The profiling of proteolytic activity shows its capacity to inhibit thrombin in the micromolar range (0.2 to 1 µM) and in the presence of heparin this inhibition was clearly increased. It was also able to inhibit Kallikrein, FXIa and slightly FXIIa, with no significant effect on other factors. In addition, the rDromaserpin inhibited thrombin-induced platelet aggre-gation. Taken together, our data suggest that rDromaserpin deserves to be further investigated as a potential candidate for developing therapeutic compounds targeting disorders related to blood clotting and/or platelet aggregation.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/EF20_079%2F0017809" target="_blank" >EF20_079/0017809: Marie Curie Fellowships - Bensaoud, Salomaki, Horváthová</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Toxins
ISSN
2072-6651
e-ISSN
2072-6651
Volume of the periodical
13
Issue of the periodical within the volume
12
Country of publishing house
CH - SWITZERLAND
Number of pages
24
Pages from-to
913
UT code for WoS article
000744660500001
EID of the result in the Scopus database
2-s2.0-85121580002