Evidence map›Paper›PMID 23954365›Full record

ArticleMolecular and biochemical parasitology2013

Identification of a family of four UDP-polypeptide N-acetylgalactosaminyl transferases in Cryptosporidium species.

Najma Bhat, Boguslaw S Wojczyk, Maria DeCicco, Carlos Castrodad, Steven L Spitalnik, Honorine D Ward

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and biochemical parasitology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. ProteinParasitology · 2019
    Review
  3. Asparagine-Linked Glycans ofMolecular & cellular proteomics : MCP · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. Review
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

6 authors at 4 institutions in 2 countries.

Najma BhatTufts Medical Center, Boston, MA, United States.
Boguslaw S Wojczyk *Department of Pathology and Cell Biology, College of Physicians and Surgeons of Columbia University, New York, NY, United States.
Maria DeCicco *Tufts Medical Center, Boston, MA, United States.
Carlos CastrodadUniversity of Puerto Rico, Cayey, PR, United States.
Steven L SpitalnikDepartment of Pathology and Cell Biology, College of Physicians and Surgeons of Columbia University, New York, NY, United States.
Honorine D WardTufts Medical Center, Boston, MA, United States.
Columbia University · USTufts University · USTufts Medical Center · USUniversity of Puerto Rico at Cayey · PR

Funding

IMMUNOLOGIC ASPECTS OF DISEASET32AI007077 · NIAID · TUFTS UNIVERSITY BOSTON · PI WORTIS, HENRY H. · 1985 to 2017
$3.5M
Building Diversity in Biomedical SciencesR25HL007785 · NHLBI · TUFTS UNIVERSITY BOSTON · PI MAGUIRE, JAMIE LYNN · 2008 to 2024
$2.0M
Molecular Basis of Crytosporidium-Host cell InteractionR01AI052786 · NIAID · TUFTS MEDICAL CENTER · PI WARD, HONORINE D · 2003 to 2007
$1.8M
O-Glycan Synthesis: Potential Targets for Intervention in CryptosporidiosisR21AI102813 · NIAID · TUFTS MEDICAL CENTER · PI WARD, HONORINE D · 2012 to 2013
$423k
NHLBI NIH HHS R25 HL007785NIAID NIH HHS R01 AI052786NIAID NIH HHS R01 AI52786NIAID NIH HHS R21 AI102813NIAID NIH HHS T32 AI007077NIAID NIH HHS T32 AI07077
6 · The paper itself

Abstract

Although mucin-type O-glycans are critical for Cryptosporidium infection, the enzymes catalyzing their synthesis have not been studied. Here, we report four UDP N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyl transferases (ppGalNAc-Ts) from the genomes of C. parvum, C. hominis and C. muris. All are Type II membrane proteins which include a cytoplasmic tail, a transmembrane domain, a stem region, a glycosyltransferase family 2 domain and a C-terminal ricin B lectin domain. All are expressed during C. parvum infection in vitro, with Cp-ppGalNAc-T1 and -T4 expressed at 24 h and Cp-ppGalNAc-T2 and -T3 at 48 and 72 h post-infection, suggesting that their expression may be developmentally regulated. C. parvum sporozoite lysates display ppGalNAc-T enzymatic activity against non-glycosylated and pre-glycosylated peptides suggesting that they contain enzymes capable of glycosylating both types of substrates. The importance of mucin-type O-glycans in Cryptosporidium-host cell interactions raises the possibility that Cp-ppGalNAc-Ts may serve as targets for intervention in cryptosporidiosis.

Indexed as

CryptosporidiumDNA, ProtozoanGene Expression ProfilingMembrane ProteinsMolecular Sequence DataN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseProtein Structure, TertiarySequence Analysis, DNADNA, ProtozoanMembrane ProteinsN-AcetylgalactosaminyltransferasesPolypeptide N-acetylgalactosaminyltransferaseCryptosporidiumMucinMucin-like glycoproteinO-glycosylationUDP GalNAc:polypeptide N-acetylgalactosaminyl transferase

Identifiers

PMID23954365
PMCPMC3856541
OpenAlexW1977696631

What OpenQuestion holds

Textmetadata
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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.