Evidence map›Paper›PMID 25931509›Full record

ArticleMolecular & cellular proteomics : MCP2015

Architecture of a Host-Parasite Interface: Complex Targeting Mechanisms Revealed Through Proteomics.

Catarina Gadelha, Wenzhu Zhang, James W Chamberlain, Brian T Chait, Bill Wickstead, Mark C Field

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Drug resistance in animal trypanosomiases: Epidemiology, mechanisms and control strategies.International journal for parasitology. Drugs and drug resistance · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Fatty acid uptake inFrontiers in cellular and infection microbiology · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Single-cell RNA sequencing ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  20. Cellular landmarks of Trypanosoma brucei and Leishmania mexicana.Molecular and biochemical parasitology · 2019
    Article
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

6 authors at 3 institutions in 2 countries.

Catarina GadelhaFrom the ‡School of Life Sciences, University of Nottingham, Nottingham, UK, NG2 7UH; §Department of Pathology, University of Cambridge, Cambridge, UK, CB2 1QP; catarina.gadelha@nottingham.ac.uk.
Wenzhu Zhang¶Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, 10021;
James W ChamberlainFrom the ‡School of Life Sciences, University of Nottingham, Nottingham, UK, NG2 7UH;
Brian T Chait¶Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, 10021;
Bill WicksteadFrom the ‡School of Life Sciences, University of Nottingham, Nottingham, UK, NG2 7UH;
Mark C Field‖Division of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, UK, DD1 5EH.
University of Nottingham · GBRockefeller University · USUniversity of Dundee · GB

Funding

National Resource for Mass Spectrom of Biological MacromoleculesP41GM103314 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2012 to 2017
$9.9M
New Tools for Exploring the Dynamic Interactome (Renewal)U54GM103511 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2012 to 2013
$6.2M
Biotechnology and Biological Sciences Research Council BB/J01477X/1Medical Research Council G0900255NIGMS NIH HHS GM103314NIGMS NIH HHS GM103511NIGMS NIH HHS P41 GM103314NIGMS NIH HHS U54 GM103511Wellcome Trust 090007/Z/09/Z
6 · The paper itself

Abstract

Surface membrane organization and composition is key to cellular function, and membrane proteins serve many essential roles in endocytosis, secretion, and cell recognition. The surface of parasitic organisms, however, is a double-edged sword; this is the primary interface between parasites and their hosts, and those crucial cellular processes must be carried out while avoiding elimination by the host immune defenses. For extracellular African trypanosomes, the surface is partitioned such that all endo- and exocytosis is directed through a specific membrane region, the flagellar pocket, in which it is thought the majority of invariant surface proteins reside. However, very few of these proteins have been identified, severely limiting functional studies, and hampering the development of potential treatments. Here we used an integrated biochemical, proteomic and bioinformatic strategy to identify surface components of the human parasite Trypanosoma brucei. This surface proteome contains previously known flagellar pocket proteins as well as multiple novel components, and is significantly enriched in proteins that are essential for parasite survival. Molecules with receptor-like properties are almost exclusively parasite-specific, whereas transporter-like proteins are conserved in model organisms. Validation shows that the majority of surface proteome constituents are bona fide surface-associated proteins and, as expected, most present at the flagellar pocket. Moreover, the largest systematic analysis of trypanosome surface molecules to date provides evidence that the cell surface is compartmentalized into three distinct domains with free diffusion of molecules in each, but selective, asymmetric traffic between. This work provides a paradigm for the compartmentalization of a cell surface and a resource for its analysis.

Indexed as

Host-Pathogen InteractionsAnimalsCell MembraneComputational BiologyHumansMass SpectrometryMembrane ProteinsParasitesProtein Structure, TertiaryProtein TransportProteomeProteomicsProtozoan ProteinsReproducibility of ResultsTrypanosoma brucei bruceiMembrane ProteinsProteomeProtozoan Proteins

Identifiers

PMID25931509
PMCPMC4587319
OpenAlexW2121458226

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.