Evidence map›Paper›PMID 27582258›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2016

Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.

Jan D Warncke, Ioannis Vakonakis, Hans-Peter Beck

Abstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

36 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
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  8. Article
  9. Comparative analysis of codon usage patterns ofFrontiers in microbiology · 2023
    Article
  10. Article
  11. Article
  12. Differential Trafficking and Expression of PIR Proteins in Acute and ChronicFrontiers in cellular and infection microbiology · 2022
    Article
  13. Adapt or Die: Targeting Unique Transmission-Stage Biology for Malaria Elimination.Frontiers in cellular and infection microbiology · 2022
    Review
  14. Article
  15. Review
  16. Review
  17. Article
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  19. Article
  20. Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x.Acta crystallographica. Section F, Structural biology communications · 2020
    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.

Jan D WarnckeSwiss Tropical and Public Health Institute, Basel, Switzerland University of Basel, Basel, Switzerland.
Ioannis VakonakisDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Hans-Peter BeckSwiss Tropical and Public Health Institute, Basel, Switzerland University of Basel, Basel, Switzerland hans-peter.beck@unibas.ch.ORCID 0000-0001-8326-4834

Funding

Medical Research Council MR/N009274/1Wellcome TrustWellcome Trust 088497/Z/09/Z
6 · The paper itself

Abstract

During the asexual cycle, Plasmodium falciparum extensively remodels the human erythrocyte to make it a suitable host cell. A large number of exported proteins facilitate this remodeling process, which causes erythrocytes to become more rigid, cytoadherent, and permeable for nutrients and metabolic products. Among the exported proteins, a family of 89 proteins, called the Plasmodium helical interspersed subtelomeric (PHIST) protein family, has been identified. While also found in other Plasmodium species, the PHIST family is greatly expanded in P. falciparum. Although a decade has passed since their first description, to date, most PHIST proteins remain uncharacterized and are of unknown function and localization within the host cell, and there are few data on their interactions with other host or parasite proteins. However, over the past few years, PHIST proteins have been mentioned in the literature at an increasing rate owing to their presence at various localizations within the infected erythrocyte. Expression of PHIST proteins has been implicated in molecular and cellular processes such as the surface display of PfEMP1, gametocytogenesis, changes in cell rigidity, and also cerebral and pregnancy-associated malaria. Thus, we conclude that PHIST proteins are central to host cell remodeling, but despite their obvious importance in pathology, PHIST proteins seem to be understudied. Here we review current knowledge, shed light on the definition of PHIST proteins, and discuss these proteins with respect to their localization and probable function. We take into consideration interaction studies, microarray analyses, or data from blood samples from naturally infected patients to combine all available information on this protein family.

Indexed as

Amino Acid SequenceErythrocytesHost-Parasite InteractionsHumansMalaria, FalciparumPlasmodium falciparumProtozoan ProteinsProtozoan Proteins

Identifiers

PMID27582258
PMCPMC5116875

What OpenQuestion holds

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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.