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Effect of different serine protease inhibitors in validating the 115 kDa <i style="mso-bidi-font-style:normal">Leishmania donovani </i>secretory serine protease as chemotherapeutic target

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Title Effect of different serine protease inhibitors in validating the 115 kDa Leishmania donovani secretory serine protease as chemotherapeutic target
 
Creator Chakraborti, Tapati
Das, Partha
Choudhury, Rajdeep
De, Tripti
 
Subject Leishmania donovani
Serine protease
Serine protease inhibitors
Anti-leishmanial activity
 
Description 14-22
Proteases have
been considered as an important group of targets for development of
antiprotozoal drugs due to their essential roles in host-parasite interactions,
parasite immune evasion, life cycle transition and pathogenesis of parasitic
diseases. The development of potent and selective serine protease inhibitors
targeting L. donovani secretory
serine protease (pSP) could pave the way to the discovery of potential
antileishmanial drugs. Here, we employed different classical serine protease
inhibitors (SPIs), such as aprotinin, N-tosyl-l-phenylalanine chloromethyl
ketone (TPCK), N-tosyl-lysine chloromethyl ketone (TLCK), benzamidine (Bza) and
pSP-antibody to determine the role of the protease in parasitic survival,
growth and infectivity. Among the different classical SPIs, aprotinin appeared
to be more potent in arresting L.
donovani promastigotes growth with significant morphological alterations.
Furthermore, aprotinin and anti-pSP treated parasites significantly decreased
the intracellular parasites and percentage of infected macrophages. These
results suggest that SPIs may reduce
the infectivity by targeting the serine protease activity and may prove useful
to elucidate defined molecular mechanisms of pSP, as well as for the
development of novel antileishmanial drugs in future.
 
Date 2015-03-30T04:39:05Z
2015-03-30T04:39:05Z
2015-02
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/31259
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.52(1) [February 2015]