Identification and Mechanistic Analysis of a Novel Tick-Derived Inhibitor of Thrombin

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F15%3A00451374" target="_blank" >RIV/60077344:_____/15:00451374 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1371/journal.pone.0133991" target="_blank" >http://dx.doi.org/10.1371/journal.pone.0133991</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0133991" target="_blank" >10.1371/journal.pone.0133991</a>

Result language

angličtina

Original language name

Identification and Mechanistic Analysis of a Novel Tick-Derived Inhibitor of Thrombin

Original language description

A group of peptides from the salivary gland of the tick Hyalomma marginatum rufipes, a vector of Crimean Congo hemorrhagic fever show weak similarity to the madanins, a group of thrombin-inhibitory peptides from a second tick species, Haemaphysalis longicornis. We have evaluated the anti-serine protease activity of one of these H. marginatum peptides that has been given the name hyalomin-1. Hyalomin-1 was found to be a selective inhibitor of thrombin, blocking coagulation of plasma and inhibiting S2238hydrolysis in a competitive manner with an inhibition constant (Ki) of 12 nM at an ionic strength of 150 mM. It also blocks the thrombin-mediated activation of coagulation factor XI, thrombin-mediated platelet aggregation, and the activation of coagulation factor V by thrombin. Hyalomin-1 is cleaved at a canonical thrombin cleavage site but the cleaved products do not inhibit coagulation. However, the C-terminal cleavage product showed non-competitive inhibition of S2238 hydrolysis. A pe

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

<a href="/en/project/GAP502%2F12%2F2409" target="_blank" >GAP502/12/2409: Investigating the role of tick salivary protease inhibitors at the interface between ticks, pathogens and the vertebrate host</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

PLoS ONE

ISSN

1932-6203

e-ISSN

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Volume of the periodical

10

Issue of the periodical within the volume

8

Country of publishing house

US - UNITED STATES

Number of pages

16

Pages from-to

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UT code for WoS article

000359061400061

EID of the result in the Scopus database

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