Evidence map›Paper›PMID 24475195›Full record

ArticlePloS one2014

Profiling of glycan receptors for minute virus of mice in permissive cell lines towards understanding the mechanism of cell recognition.

Sujata Halder, Susan Cotmore, Jamie Heimburg-Molinaro, David F Smith, Richard D Cummings, Xi Chen, Alana J Trollope, Simon J North, Stuart M Haslam, Anne Dell and 3 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Parvovirus glycan interactions.Current opinion in virology · 2014
    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

13 authors at 5 institutions in 2 countries.

Sujata HalderDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida, United States of America.
Susan CotmoreDepartment of Laboratory Medicine, Yale School of Medicine, New Haven, Connecticut, United States of America.
Jamie Heimburg-MolinaroDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America.
David F SmithDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Richard D CummingsDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Xi ChenDepartment of Chemistry, University of California Davis, Davis, California, United States of America.
Alana J TrollopeDivision of Molecular Biosciences, Imperial College London, London, United Kingdom.
Simon J NorthDivision of Molecular Biosciences, Imperial College London, London, United Kingdom.
Stuart M HaslamDivision of Molecular Biosciences, Imperial College London, London, United Kingdom.
Anne DellDivision of Molecular Biosciences, Imperial College London, London, United Kingdom.
Peter TattersallDepartment of Laboratory Medicine, Yale School of Medicine, New Haven, Connecticut, United States of America.
Robert McKennaDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida, United States of America.
Mavis Agbandje-McKennaDepartment of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida, United States of America.
Imperial College London · GBEmory University · USUniversity of Florida · USYale University · USUniversity of California, Davis · US

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BLIXT, OLA KLAS · 2001 to 2010
$80.3M
MOLECULAR BASIS OF PARVOVIRUS TARGET CELL SPECIFICITYR01CA029303 · NCI · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 1985 to 2016
$7.5M
Overall Priority Score P41GM103694 · NIGMS · EMORY UNIVERSITY · PI CUMMINGS, RICHARD D · 2013 to 2018
$6.9M
Shotgun Glycomics: Linking Glycan Structure and FunctionR01GM085448 · NIGMS · EMORY UNIVERSITY · PI SMITH, DAVID FLETCHER · 2008 to 2011
$2.3M
Studies of Naturally Occurring Structurally Modified CarbohydratesR01GM076360 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2006 to 2010
$1.9M
Biotechnology and Biological Sciences Research Council BB/F008309/1NCI NIH HHS CA029303NCI NIH HHS R01 CA029303NIGMS NIH HHS GM076360NIGMS NIH HHS GM085448NIGMS NIH HHS P41 GM103694NIGMS NIH HHS R01 GM076360NIGMS NIH HHS R01 GM085448NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

The recognition of sialic acids by two strains of minute virus of mice (MVM), MVMp (prototype) and MVMi (immunosuppressive), is an essential requirement for successful infection. To understand the potential for recognition of different modifications of sialic acid by MVM, three types of capsids, virus-like particles, wild type empty (no DNA) capsids, and DNA packaged virions, were screened on a sialylated glycan microarray (SGM). Both viruses demonstrated a preference for binding to 9-O-methylated sialic acid derivatives, while MVMp showed additional binding to 9-O-acetylated and 9-O-lactoylated sialic acid derivatives, indicating recognition differences. The glycans recognized contained a type-2 Galβ1-4GlcNAc motif (Neu5Acα2-3Galβ1-4GlcNAc or 3'SIA-LN) and were biantennary complex-type N-glycans with the exception of one. To correlate the recognition of the 3'SIA-LN glycan motif as well as the biantennary structures to their natural expression in cell lines permissive for MVMp, MVMi, or both strains, the N- and O-glycans, and polar glycolipids present in three cell lines used for in vitro studies, A9 fibroblasts, EL4 T lymphocytes, and the SV40 transformed NB324K cells, were analyzed by MALDI-TOF/TOF mass spectrometry. The cells showed an abundance of the sialylated glycan motifs recognized by the viruses in the SGM and previous glycan microarrays supporting their role in cellular recognition by MVM. Significantly, the NB324K showed fucosylation at the non-reducing end of their biantennary glycans, suggesting that recognition of these cells is possibly mediated by the Lewis X motif as in 3'SIA-Le(X) identified in a previous glycan microarray screen.

Indexed as

AnimalsCapsidCell LineFibroblastsHumansLymphocytesMiceMicroarray AnalysisMinute Virus of MiceN-Acetylneuraminic AcidSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationVirionN-Acetylneuraminic Acid

Identifiers

PMID24475195
PMCPMC3903596
OpenAlexW2033084143

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.