Evidence map›Paper›PMID 26950937›Full record

ArticlePloS one2016

Identification of Novel O-Linked Glycosylated Toxoplasma Proteins by Vicia villosa Lectin Chromatography.

Kevin Wang, Eric D Peng, Amy S Huang, Dong Xia, Sarah J Vermont, Gaelle Lentini, Maryse Lebrun, Jonathan M Wastling, Peter J Bradley

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 41 citations in OpenAlex.

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  10. Review
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  12. Review
  13. ProteinParasitology · 2019
    Review
  14. Article
  15. CRISPR/Cas9 and glycomics tools forThe Journal of biological chemistry · 2019
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. 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

9 authors at 5 institutions in 3 countries.

Kevin WangDepartment of Microbiology, Immunology and Molecular Genetics, University of California Los Angeles, Los Angeles, California, 90095-1489, United States of America.
Eric D PengDepartment of Microbiology, Immunology and Molecular Genetics, University of California Los Angeles, Los Angeles, California, 90095-1489, United States of America.
Amy S HuangDepartment of Microbiology, Immunology and Molecular Genetics, University of California Los Angeles, Los Angeles, California, 90095-1489, United States of America.
Dong XiaInstitute of Infection and Global Health, University of Liverpool, Liverpool, United Kingdom.
Sarah J VermontInstitute of Infection and Global Health, University of Liverpool, Liverpool, United Kingdom.
Gaelle LentiniUMR 5235 CNRS, Université de Montpellier 1 and 2, 34095, Montpellier, France.
Maryse LebrunUMR 5235 CNRS, Université de Montpellier 1 and 2, 34095, Montpellier, France.
Jonathan M WastlingFaculty of Natural Sciences, University of Keele, Staffordshire, United Kingdom.
Peter J BradleyDepartment of Microbiology, Immunology and Molecular Genetics, University of California Los Angeles, Los Angeles, California, 90095-1489, United States of America.
University of California, Los Angeles · USUniversity of Liverpool · GBCentre National de la Recherche Scientifique · FRKeele University · GBUniversité de Montpellier · FR

Funding

The Role of Toxoplasma Rhoptries in Host Cell InfectionR01AI064616 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BRADLEY, PETER JOHN · 2006 to 2016
$3.5M
Biotechnology and Biological Sciences Research Council BBS/B/08493NIAID NIH HHS AI064616NIAID NIH HHS R01 AI064616
6 · The paper itself

Abstract

Toxoplasma gondii maintains its intracellular life cycle using an extraordinary arsenal of parasite-specific organelles including the inner membrane complex (IMC), rhoptries, micronemes, and dense granules. While these unique compartments play critical roles in pathogenesis, many of their protein constituents have yet to be identified. We exploited the Vicia villosa lectin (VVL) to identify new glycosylated proteins that are present in these organelles. Purification of VVL-binding proteins by lectin affinity chromatography yielded a number of novel proteins that were subjected to further study, resulting in the identification of proteins from the dense granules, micronemes, rhoptries and IMC. We then chose to focus on three proteins identified by this approach, the SAG1 repeat containing protein SRS44, the rhoptry neck protein RON11 as well as a novel IMC protein we named IMC25. To assess function, we disrupted their genes by homologous recombination or CRISPR/Cas9. The knockouts were all successful, demonstrating that these proteins are not essential for invasion or intracellular survival. We also show that IMC25 undergoes substantial proteolytic processing that separates the C-terminal domain from the predicted glycosylation site. Together, we have demonstrated that lectin affinity chromatography is an efficient method of identifying new glycosylated parasite-specific proteins.

Indexed as

ChromatographyToxoplasmaAcetylgalactosamineCell MembraneGlycosylationPlant LectinsProteolysisProtozoan ProteinsVacuolesAcetylgalactosaminePlant LectinsProtozoan ProteinsVicia lectins

Identifiers

PMID26950937
PMCPMC4780768
OpenAlexW2295952587

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.