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Identification and characterization of cysteine proteinases of Trypanosoma evansi

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Title Identification and characterization of cysteine proteinases of Trypanosoma evansi
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Creator S. C. Yadav & R. Kumar & S. Kumar & U. Tatu & R. K. Singh & A. K. Gupta
 
Subject Trypanosoma evansi
 
Description Not Available
Trypanosoma evansi is a causative agent of
‘surra’, a common haemoprotozoan disease of livestock in
India causing high morbidity and mortality in disease
endemic areas. The proteinases released by live and dead
trypanosomes entail immunosuppression in the infected
host, which immensely contribute in disease pathogenesis.
Cysteine proteinases are identified in the infectious cycle
of trypanosomes such as cruzain from Trypanosoma
cruzi, rhodesain or brucipain from Trypanosoma brucei
rhodesiense and congopain from Trypanosoma congelense.
These enzymes localised in lysosome-like organelles,
flagellar pocket and on cell surface, which play a
critical role in the life cycle of protozoan parasites, viz. in
host invasion, nutrition and alteration of the host immune
response. The paper describes the identification of cysteine
proteinases of T. evansi lysate, activity profile at
different pH optima and inhibition pattern using a specific
inhibitor, besides the polypeptide profile of an antigen.
Eight proteinases of T. evansi were identified in the
molecular weight (MW) ranges of 28–170 kDa using
gelatin substrate-polyacrylamide gel electrophoresis
(GS-PAGE), and of these proteinases, six were cysteine
proteinases, as they were inhibited by L-3-carboxy-2,3-
transepoxypropionyl-lecuylamido (4-guanidino)-butane
(E-64), a specific inhibitor. These proteolytic enzymes
were most reactive in acidic pH between 3.0 and 5.5 in the
presence of dithiothreitol and completely inactive at
alkaline pH 10.0. Similarly, the GS-PAGE profile of the
serum samples of rats infected with T. evansi revealed
strong proteolytic activity only at the 28-kDa zone at
pH 5.5, while no proteolytic activity was observed in
serum samples of uninfected rats. Further, the other zones
of clearance, which were evident in T. evansi antigen
zymogram, could not be observed in the serum samples of
rats infected with T. evansi. The polypeptide pattern of the
whole cell lysate antigen revealed 12–15 polypeptide
bands ranging from 28 to 81 kDa along with five
predominant polypeptides bands (MW of 81, 66, 62, 55
and 45 kDa), which were immunoreactive with hyperimmune
serum (HIS) and serum of experimentally infected
rabbits with T. evansi infection. The immunoblot recognised
antibodies in experimentally infected rabbits and
against HIS as well, corresponding to the zone of
clearances at lower MW ranges (28–41 kDa), which may
be attributed to the potential of these proteinases in the
diagnosis of T. evansi infection. Since these thioldependent
enzymes are most active in acidic pH and
considering their inhibition characteristics, these data
suggest that they resemble to the mammalian lysosomal
cathepsin B and L.
Not Available
 
Date 2019-12-05T11:02:47Z
2019-12-05T11:02:47Z
2011-02-25
 
Type Book
 
Identifier Not Available
DOI 10.1007/s00436-011-2284-9
http://krishi.icar.gov.in/jspui/handle/123456789/28168
 
Language English
 
Relation Not Available;
 
Publisher Not Available