Evidence map›Paper›PMID 18559479›Full record

ArticleGenes & development2008

An Entamoeba histolytica rhomboid protease with atypical specificity cleaves a surface lectin involved in phagocytosis and immune evasion.

Leigh A Baxt, Rosanna P Baker, Upinder Singh, Sinisa Urban

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–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

53 citing papers in PubMed, 96 citations in OpenAlex.

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  7. Life (Basel, Switzerland) · 2021
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  8. Taxon-Specific Proteins of the PathogenicFrontiers in cellular and infection microbiology · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Leigh A BaxtDepartment of Internal Medicine and Microbiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Rosanna P Baker
Upinder Singh
Sinisa Urban
Johns Hopkins University · USStanford University · US

Funding

MOLECULAR BASIS OF HOST-PARASITE INTERACTIONT32AI007328 · NIAID · STANFORD UNIVERSITY · PI JUSTIN L SONNENBURG · 1987 to 2026
$11.9M
Biochemistry of Intramembrane Proteases From PathogensR01AI066025 · NIAID · JOHNS HOPKINS UNIVERSITY · PI NATHANS, JEREMY · 2005 to 2019
$4.9M
Investigating Entamoeba histolytica Colonic PathogenesisR01AI053724 · NIAID · STANFORD UNIVERSITY · PI SINGH, UPINDER · 2003 to 2012
$3.8M
NIAID NIH HHS AI-053724NIAID NIH HHS R01 AI053724NIAID NIH HHS R01 AI066025NIAID NIH HHS R01AI066025NIAID NIH HHS T32 AI007328NIAID NIH HHS T32-AI07328Wellcome Trust
6 · The paper itself

Abstract

Rhomboid proteases are membrane-embedded enzymes conserved in all kingdoms of life, but their cellular functions across evolution are largely unknown. Prior work has uncovered a role for rhomboid enzymes in host cell invasion by malaria and related intracellular parasites, but this is unlikely to be a widespread function, even in pathogens, since rhomboid proteases are also conserved in unrelated protozoa that maintain an extracellular existence. We examined rhomboid function in Entamoeba histolytica, an extracellular, parasitic ameba that is second only to malaria in medical burden globally. Despite its large genome, E. histolytica encodes only one rhomboid (EhROM1) with residues necessary for protease activity. EhROM1 displayed atypical substrate specificity, being able to cleave Plasmodium adhesins but not the canonical substrate Drosophila Spitz. We searched for substrates encoded in the ameba genome and found EhROM1 was able to cleave a cell surface lectin specifically. In E. histolytica trophozoites, EhROM1 changed localization to vesicles during phagocytosis and to the posterior cap structure during surface receptor shedding for immune evasion, in both cases colocalizing with lectins. Collectively these results implicate rhomboid proteases for the first time in immune evasion and suggest that a common function of rhomboid enzymes in widely divergent protozoan pathogens is to break down adhesion proteins.

Indexed as

Amino Acid SequenceAnimalsAntigens, ProtozoanAntigens, SurfaceCell Adhesion MoleculesChlorocebus aethiopsCOS CellsEntamoeba histolyticaHost-Parasite InteractionsImmune ToleranceLectinsMolecular Sequence DataPeptide HydrolasesPhagocytosisPlasmodiumProtozoan ProteinsAntigens, ProtozoanAntigens, SurfaceCell Adhesion MoleculesLectinsPeptide HydrolasesProtozoan ProteinsROM4 protein, Plasmodium falciparum

Identifiers

PMID18559479
PMCPMC2428061
OpenAlexW2123345044

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.