Evidence map›Paper›PMID 25924022›Full record

ArticleCellular microbiology2015

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

Jean-Mathieu Bart, Carlos Cordon-Obras, Isabel Vidal, Jennifer Reed, Esperanza Perez-Pastrana, Laureano Cuevas, Mark C Field, Mark Carrington, Miguel Navarro

Open access · bronzeAbstract read
In one paragraph

Article in Cellular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Autophagic-related cell death of Trypanosoma brucei induced by bacteriocin AS-48.International journal for parasitology. Drugs and drug resistance · 2018
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  2. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 6 institutions in 2 countries.

Jean-Mathieu BartInstituto de Parasitología y Biomedicina 'López-Neyra', Consejo Superior de Investigaciones Científicas, Granada, Spain.
Carlos Cordon-ObrasInstituto de Parasitología y Biomedicina 'López-Neyra', Consejo Superior de Investigaciones Científicas, Granada, Spain.
Isabel VidalInstituto de Parasitología y Biomedicina 'López-Neyra', Consejo Superior de Investigaciones Científicas, Granada, Spain.
Jennifer ReedDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Esperanza Perez-PastranaCentro Nacional de Microbiología, Instituto de Salud Carlos III, Madrid, Spain.
Laureano CuevasCentro Nacional de Microbiología, Instituto de Salud Carlos III, Madrid, Spain.
Mark C FieldDivision of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, UK.
Mark CarringtonDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Miguel NavarroInstituto de Parasitología y Biomedicina 'López-Neyra', Consejo Superior de Investigaciones Científicas, Granada, Spain.
Consejo Superior de Investigaciones Científicas · ESInstituto de Parasitología y Biomedicina "López - Neyra" · ESUniversity of Cambridge · GBCentro Nacional de Microbiologia · ESInstituto de Salud Carlos III · ESUniversity of Dundee · GB

Funding

LCenter for Clinical and Translational Science and TrainingUL1TR001425 · NCATS · UNIVERSITY OF CINCINNATI · PI MEINZEN-DERR, JAREEN, STRAWN, JEFFREY ROBERT · 2015 to 2024
$37.5M
Medical Research CouncilWellcome Trust 090007Wellcome Trust 093008Wellcome Trust 093008/Z/10/Z
6 · The paper itself

Abstract

African 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 ≈ 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.

Indexed as

AnimalsApolipoprotein L1ApolipoproteinsEndosomesHumansLipoproteins, HDLLysosomesMembrane GlycoproteinsMicroscopy, FluorescenceMicroscopy, ImmunoelectronProtozoan ProteinsTrypanosoma brucei bruceiTrypanosoma brucei rhodesienseAPOL1 protein, humanApolipoprotein L1ApolipoproteinsLipoproteins, HDLMembrane GlycoproteinsProtozoan Proteinsserum resistance associated protein, Trypanosoma brucei

Identifiers

PMID25924022
PMCPMC6736673
OpenAlexW2154165298

What Socratic holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.