Evidence map›Paper›PMID 27840079›Full record

ArticleMolecular and biochemical parasitology2017

Glucosylceramide transferase in Giardia preferentially catalyzes the synthesis of galactosylceramide during encystation.

Leobarda Robles-Martinez, Tavis L Mendez, Jennifer Apodaca, Siddhartha Das

Open access · greenAbstract read
In one paragraph

Article in Molecular and biochemical parasitology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 35% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Leobarda Robles-Martinez *Infectious Disease and Immunology Cluster, Border Biomedical Research Center (BBRC), University of Texas at El Paso, El Paso, TX 79968-0519, USA; Department of Biological Sciences, University of Texas at El Paso, 500 W. University Avenue, El Paso, TX 79968-0519/USA, Tel: (915) 747-6896∥.
Tavis L Mendez *Infectious Disease and Immunology Cluster, Border Biomedical Research Center (BBRC), University of Texas at El Paso, El Paso, TX 79968-0519, USA; Department of Biological Sciences, University of Texas at El Paso, 500 W. University Avenue, El Paso, TX 79968-0519/USA, Tel: (915) 747-6896∥.
Jennifer ApodacaInfectious Disease and Immunology Cluster, Border Biomedical Research Center (BBRC), University of Texas at El Paso, El Paso, TX 79968-0519, USA; Department of Biological Sciences, University of Texas at El Paso, 500 W. University Avenue, El Paso, TX 79968-0519/USA, Tel: (915) 747-6896∥.
Siddhartha DasInfectious Disease and Immunology Cluster, Border Biomedical Research Center (BBRC), University of Texas at El Paso, El Paso, TX 79968-0519, USA; Department of Biological Sciences, University of Texas at El Paso, 500 W. University Avenue, El Paso, TX 79968-0519/USA, Tel: (915) 747-6896∥.
The University of Texas at El Paso · USBorder Network for Human Rights · US

Funding

TCCG12MD007592 · NIMHD · UNIVERSITY OF TEXAS EL PASO · PI KIRKEN, ROBERT A. · 2012 to 2018
$19.4M
Sphingolipid and Mechanism of Cyst Formation by GiardiaR01AI095667 · NIAID · UNIVERSITY OF TEXAS EL PASO · PI DAS, SIDDHARTHA · 2011 to 2015
$2.1M
NIAID NIH HHS R01 AI095667NIMHD NIH HHS G12 MD007592
6 · The paper itself

Abstract

The stage differentiation from trophozoite to cyst (i.e., encystation) is an essential step for Giardia to survive outside its human host and spread the infection via the fecal-oral route. We have previously shown that Giardia expresses glucosylceramide transferase 1 (GlcT1) enzyme, the activity of which is elevated during encystation. We have also reported that blocking the activity of gGlcT1 interferes with the biogenesis of encystation-specific vesicles (ESVs) and cyst viability in Giardia. To further understand the role of this enzyme and how it regulates encystation, we overexpressed, knocked down, and rescued the giardial GlcT1 (gGlcT1) gene and measured its enzymatic activity in live parasites as well as in isolated membrane fractions using NBD-ceramide and UDP-glucose or UDP-galactose. We observed that gGlcT1 is able to catalyze the synthesis of both glucosylceramide (GlcCer) and galactosylceramide (GalCer), however the synthesis of GalCer is 2-3 fold higher than of GlcCer. Although both activities follow Michaelis-Menten kinetics, the bindings of UDP-glucose and UDP-galactose with the enzyme appear to be non-competitive and independent of each other. The modulation of gGlcT1 synthesis concomitantly influenced the expression cyst-wall protein (CWP) and overall encystation. We propose that gGlcT1 is a unique enzyme and that Giardia uses this enzyme to synthesize both GlcCer and GalCer to facilitate the process of encystation/cyst production.

Indexed as

Amino Acid SequenceEnzyme ActivationGene ExpressionGene Knockdown TechniquesGiardiaGiardiasisGlucosylceramidesGlycosylationKineticsProtein DomainsProtozoan ProteinsSubstrate SpecificityTransferasesGlucosylceramidesProtozoan ProteinsTransferasesAnti-sense morpholino oligonucleotideEncystationGalactosylceramideGiardia lambliaGlucosylceramideGlucosylceramide transferaseSphingolipid

Identifiers

PMID27840079
PMCPMC5222682
OpenAlexW2555402553

What OpenQuestion holds

Textmetadata
LicenceTDM
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.