Evidence map›Paper›PMID 19805524›Full record

ArticleInfection and immunity2009

Molecular characterization of EmABP, an apolipoprotein A-I binding protein secreted by the Echinococcus multilocularis metacestode.

Peter Bernthaler, Kerstin Epping, Gerd Schmitz, Peter Deplazes, Klaus Brehm

Abstract read
In one paragraph

Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

12 citing papers in PubMed.

  1. Host Proteins inInternational journal of molecular sciences · 2025
    Article
  2. Article
  3. Targeted and non-targeted proteomics to characterize the parasite proteins ofFrontiers in cellular and infection microbiology · 2023
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  5. Article
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  7. Review
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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

5 authors.

Peter BernthalerInstitute of Hygiene and Microbiology, University of Würzburg, D-97080 Würzburg, Germany.
Kerstin Epping
Gerd Schmitz
Peter Deplazes
Klaus Brehm

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cestodes are unable to synthesize de novo most of their own membrane lipids, including cholesterol, and have to take them up from the host during an infection. The underlying molecular mechanisms are so far unknown. Here we report the identification and characterization of a novel gene, Emabp, which is expressed by larval stages and adults of the fox tapeworm Echinococcus multilocularis. The encoded protein, EmABP, displays significant homologies to apolipoprotein A-I binding protein (AI-BP) of mammalian origin and to metazoan YjeF_N domain proteins. Like mammalian AI-BP, EmABP carries an export-directing signal sequence which is absent in predicted AI-BP orthologs from the related flatworms Schistosoma japonicum and Schmidtea mediterranea. Using a specific antibody and immunoprecipitation techniques, we demonstrate that EmABP is secreted into the extraparasitic environment and into the hydatid fluid of in vitro-cultivated metacestode vesicles. Furthermore, we show that apolipoprotein A-I (apoA-I), a major constituent of cholesterol-transporting high-density lipoproteins, is present in hydatid fluid. By pulldown experiments, we demonstrate that recombinantly expressed, purified EmABP interacts with purified human apoA-I and is able to precipitate apoA-I from human serum. On the basis of these features and the suggested function of AI-BP in cholesterol transport in higher eukaryotes, we propose a role for EmABP in cholesterol and lipid uptake mechanisms of larval E. multilocularis.

Indexed as

Amino Acid SequenceAnimalsApolipoprotein A-ICarrier ProteinsEchinococcus multilocularisHelminth ProteinsMolecular Sequence DataProtein BindingProtein Sorting SignalsSequence Homology, Amino AcidApolipoprotein A-ICarrier ProteinsHelminth ProteinsProtein Sorting Signals

Identifiers

PMID19805524
PMCPMC2786436

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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.