Excretion/secretion products from Schistosoma mansoni adults, eggs and schistosomula have unique peptidase specificity profiles

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F16%3A00471827" target="_blank" >RIV/68378050:_____/16:00471827 - isvavai.cz</a>

Alternative codes found

RIV/60077344:_____/16:00469034 RIV/61388963:_____/16:00471793 RIV/00216208:11110/16:10325212 RIV/00216208:11310/16:10325212

Result on the web

<a href="http://dx.doi.org/10.1016/j.biochi.2015.09.025" target="_blank" >http://dx.doi.org/10.1016/j.biochi.2015.09.025</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.biochi.2015.09.025" target="_blank" >10.1016/j.biochi.2015.09.025</a>

Result language

angličtina

Original language name

Excretion/secretion products from Schistosoma mansoni adults, eggs and schistosomula have unique peptidase specificity profiles

Original language description

Schistosomiasis is one of a number of chronic helminth diseases of poverty that severely impact personal and societal well-being and productivity. Peptidases (proteases) are vital to successful parasitism, and Can modulate host physiology and immunology. Interference of peptidase action by specific drugs or vaccines can be therapeutically beneficial. To date, research on peptidases in the schistosome parasite has focused on either the functional characterization of individual peptidases or their annotation as part of global genome or transcriptome studies. We were interested in functionally characterizing the complexity of peptidase activity operating at the host parasite interface, therefore the excretory secretory products of key developmental stages of Schistosoma mansoni that parasitize the human were examined. Using class specific peptidase inhibitors in combination with a multiplex substrate profiling assay, a number of unique activities derived from endo- and exo-peptidases were revealed in the excretory-secretory products of schistosomula (larval migratory worms), adults and eggs. The data highlight the complexity of the functional degradome for each developmental stage of this parasite and facilitate further enquiry to establish peptidase identity, physiological and immunological function, and utility as drug or vaccine candidates. (C) 2015 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.

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

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

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

Name of the periodical

Biochimie

ISSN

0300-9084

e-ISSN

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Volume of the periodical

122

Issue of the periodical within the volume

jaro

Country of publishing house

FR - FRANCE

Number of pages

11

Pages from-to

99-109

UT code for WoS article

000370910700010

EID of the result in the Scopus database

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