Evidence map›Paper›PMID 22383874›Full record

ArticlePLoS pathogens2012

Novel transmembrane receptor involved in phagosome transport of lysozymes and β-hexosaminidase in the enteric protozoan Entamoeba histolytica.

Atsushi Furukawa, Kumiko Nakada-Tsukui, Tomoyoshi Nozaki

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Molecular interplays of theFrontiers in cellular and infection microbiology · 2022
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  7. Article
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  11. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  12. Article
  13. Article
  14. Non-vesicular Lipid Transport Machinery inFrontiers in cellular and infection microbiology · 2018
    Review
  15. Review
  16. Entamoeba mitosomes play an important role in encystation by association with cholesteryl sulfate synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
  18. Article
  19. Regulation of virulence of Entamoeba histolytica.Annual review of microbiology · 2014
    Review
  20. The cell surface proteome of Entamoeba histolytica.Molecular & cellular proteomics : MCP · 2014
    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

3 authors at 2 institutions in 1 country.

Atsushi FurukawaDepartment of Parasitology, National Institute of Infectious Diseases, Toyama, Shinjuku-ku, Tokyo, Japan.
Kumiko Nakada-Tsukui
Tomoyoshi Nozaki
National Institute of Infectious Diseases · JPGunma University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysozymes and hexosaminidases are ubiquitous hydrolases in bacteria and eukaryotes. In phagocytic lower eukaryotes and professional phagocytes from higher eukaryotes, they are involved in the degradation of ingested bacteria in phagosomes. In Entamoeba histolytica, which is the intestinal protozoan parasite that causes amoebiasis, phagocytosis plays a pivotal role in the nutrient acquisition and the evasion from the host defense systems. While the content of phagosomes and biochemical and physiological roles of the major phagosomal proteins have been established in E. histolytica, the mechanisms of trafficking of these phagosomal proteins, in general, remain largely unknown. In this study, we identified and characterized for the first time the putative receptor/carrier involved in the transport of the above-mentioned hydrolases to phagosomes. We have shown that the receptor, designated as cysteine protease binding protein family 8 (CPBF8), is localized in lysosomes and mediates transport of lysozymes and β-hexosaminidase α-subunit to phagosomes when the amoeba ingests mammalian cells or Gram-positive bacillus Clostridium perfringens. We have also shown that the binding of CPBF8 to the cargos is mediated by the serine-rich domain, more specifically three serine residues of the domain, which likely contains trifluoroacetic acid-sensitive O-phosphodiester-linked glycan modifications, of CPBF8. We further showed that the repression of CPBF8 by gene silencing reduced the lysozyme and β-hexosaminidase activity in phagosomes and delayed the degradation of C. perfringens. Repression of CPBF8 also resulted in decrease in the cytopathy against the mammalian cells, suggesting that CPBF8 may also be involved in, besides the degradation of ingested bacteria, the pathogenesis against the mammalian hosts. This work represents the first case of the identification of a transport receptor of hydrolytic enzymes responsible for the degradation of microorganisms in phagosomes.

Indexed as

Amino Acid SequenceAnimalsbeta-N-AcetylhexosaminidasesBiological TransportCHO CellsCricetinaeCricetulusEntamoeba histolyticaLysosomesMembrane ProteinsMolecular Sequence DataPhagocytosisPhagosomesProtein BindingProtozoan ProteinsReceptors, Cell Surfacebeta-N-AcetylhexosaminidasesMembrane ProteinsProtozoan ProteinsReceptors, Cell Surface

Identifiers

PMID22383874
PMCPMC3285589
OpenAlexW2045239662

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

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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.