4.5 Article

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

期刊

BIOCHIMIE
卷 122, 期 -, 页码 99-109

出版社

ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2015.09.025

关键词

Parasite; Fluke; Secretion; Excretion; Protease; Inhibitor

资金

  1. University of California
  2. Francisco Program for Breakthrough Biomedical Research
  3. Sandler Foundation
  4. Czech Science Foundation [P302/11/1481]
  5. FP7 Marie Curie International Reintegration Grant [248642]
  6. Ministry of Education, Youth and Sports of the Czech Republic [LO1302]
  7. institutional project [RVO 61388963]
  8. NIH-NIAID [R01AI089896, R21AI107390]
  9. Biomedical Technology Research Centers program, National Institutes of Health, National Institute of General Medical Sciences [8P41GM103481]

向作者/读者索取更多资源

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.

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