English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/182483
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:

Title

Localization of serum resistance-associated protein in Trypanosoma brucei rhodesiense and transgenic Trypanosoma brucei brucei

AuthorsBart, Jean-Mathieu; Cordon-Obras, Carlos; Vidal, Isabel; Reed, Jennifer; Perez-Pastrana, Esperanza; Cuevas, Laureano; Field, Mark C.; Carrington, Mark; Navarro, M.
Issue DateOct-2015
PublisherJohn Wiley & Sons
CitationCellular Microbiology
AbstractAfrican trypanosomes infect a broad range of mammals, but humans and some higher primates are protected by serum trypanosome lytic factors that contain apolipoprotein L1 (ApoL1). In the human-infective subspecies of Trypanosoma brucei, Trypanosoma brucei rhodesiense, a gene product derived from the variant surface glycoprotein gene family member, serum resistance-associated protein (SRA protein), protects against ApoL1-mediated lysis. Protection against trypanosome lytic factor requires the direct interaction between SRA protein and ApoL1 within the endocytic apparatus of the trypanosome, but some uncertainty remains as to the precise mechanism and location of this interaction. In order to provide more insight into the mechanism of SRA-mediated resistance to trypanosome lytic factor, we assessed the localization of SRA in T. b. rhodesiense EATRO3 using a novel monoclonal antibody raised against SRA together with a set of well-characterized endosomal markers. By three-dimensional deconvolved immunofluorescence single-cell analysis, combined with double-labelling immunoelectron microscopy, we found that approximate to 50% of SRA protein localized to the lysosome, with the remaining population being distributed through the endocytic pathway, but apparently absent from the flagellar pocket membrane. These data suggest that the SRA/trypanolytic factor interaction is intracellular, with the concentration within the endosomes potentially crucial for ensuring a high efficiency.
Publisher version (URL)http://dx.doi.org/10.1111/cmi.12454
URIhttp://hdl.handle.net/10261/182483
DOI10.1111/cmi.12454
ISSN1462-5814
E-ISSN1462-5822
Appears in Collections:(IPBLN) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,35 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.