Thumbnail
Access Restriction
Subscribed

Author Neves, Roberta F. C. ♦ Fernandes, Anne C. S ♦ Meyer Fernandes, José R ♦ Souto Padrón, Thais
Source SpringerLink
Content type Text
Publisher Springer Berlin Heidelberg
File Format PDF
Copyright Year ©2014
Language English
Subject Domain (in DDC) Technology ♦ Medicine & health
Subject Keyword Trypanosoma cruzi ♦ Membrane vesicles ♦ Shedding ♦ Secretion ♦ Phosphatase ♦ Medical Microbiology ♦ Microbiology ♦ Immunology
Abstract Trypanosoma cruzi virulence factors include molecules expressed on the cell surface as well as those secreted or shed into the extracellular medium. Phosphatase activities modulate different aspects of T. cruzi infection, although no studies to date addressed the presence and activity of phosphatases in vesicles secreted by this parasite. Here, we characterized acidic and alkaline secreted phosphatase activities of human-infective trypomastigote forms of T. cruzi from the Y strain and the CL-Brener clone. These are widely studied T. cruzi strains that represent “opposite ends of the spectrum” regarding both in vitro and in vivo behavior. Ecto-phosphatase activities were determined in live parasites, and secreted phosphatase activities were analyzed in soluble protein (SP) and vesicular membrane fractions (VFs) of parasite-conditioned medium. Our analysis using different phosphatase inhibitors strongly suggests that vesicles secreted by Y strain (VFY) and CL-Brener (VFCLB) trypomastigotes are derived mostly from the cell surface and from exosome secretion, respectively. Importantly, our results show that the acid phosphatase activities in vesicles secreted by trypomastigotes are largely responsible for the VF-induced increase in adhesion of Y strain parasites to host cells and also for the VF-induced increase in host cell infection by CL-Brener trypomastigotes.
ISSN 09320113
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2014-06-07
Publisher Place Berlin/Heidelberg
e-ISSN 14321955
Journal Parasitology Research
Volume Number 113
Issue Number 8
Page Count 12
Starting Page 2961
Ending Page 2972


Open content in new tab

   Open content in new tab
Source: SpringerLink