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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/35337
Title: Fasciola gigantica cathepsin B5 is an acidic endo- and exopeptidase of the immature and mature parasite
Authors: Sinee Siricoon
Suksiri Vichasri Grams
Kittisak Lertwongvisarn
Muntana Abdullohfakeeyah
Peter M. Smooker
Rudi Grams
Thammasat University
Mahidol University
RMIT University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Dec-2015
Citation: Biochimie. Vol.119, (2015), 6-15
Abstract: © 2015 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved. Cysteine proteases of the liver fluke Fasciola have been described as essential molecules in the infection process of the mammalian host. Destinct cathepsin Bs, which are already expressed in the metacercarial stage and released by the newly excysted juvenile are major actors in this process. Following infection their expression is stopped and the proteins will not be detectable any longer after the first month of development. On the contrary, the novel cathepsin B5 of Fasciola gigantica (FgCB5) described in this work was also found expressed in later juvenile stages and the mature worm. Like all previously described Fasciola family members it was located in the cecal epithelium of the parasite. Western blot analysis of adult antigen preparations detected procathepsin B5 in crude worm extract and in small amounts in the ES product. In support of these data, the sera of infected rabbits and mice were reactive with recombinant FgCB5 in Western blot and ELISA. Biochemical analysis of yeast-expressed FgCB5 revealed that it has properties of a lysosomal hydrolase optimized for activity at acid pH and that it is able to efficiently digest a broad spectrum of host proteins. Unlike previously characterized Fasciola family members FgCB5 carries a histidine doublet in the occluding loop equivalent to residues His110 and His111 of human mature cathepsin B and consequently showed substantial carboxydipeptidyl activity which depends on these two residues.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84944075407&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/35337
ISSN: 61831638
03009084
Appears in Collections:Scopus 2011-2015

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