Evidence map›Paper›PMID 23115247›Full record

ArticleThe Journal of biological chemistry2012

Functional glycomic analysis of human milk glycans reveals the presence of virus receptors and embryonic stem cell biomarkers.

Ying Yu, Shreya Mishra, Xuezheng Song, Yi Lasanajak, Konrad C Bradley, Mary M Tappert, Gillian M Air, David A Steinhauer, Sujata Halder, Susan Cotmore and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
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  6. Article
  7. Examining Galectin Binding Specificity Using Glycan Microarrays.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
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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

14 authors at 4 institutions in 1 country.

Ying YuDepartment of Biochemistry and the Glycomics Center, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Shreya Mishra
Xuezheng Song
Yi Lasanajak
Konrad C Bradley
Mary M Tappert
Gillian M Air
David A Steinhauer
Sujata Halder
Susan Cotmore
Peter Tattersall
Mavis Agbandje-McKenna
Richard D Cummings
David F Smith
Emory University · USUniversity of Florida · USUniversity of Oklahoma Health Sciences Center · USYale University · US

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI ORR, SALLY L · 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
Protein-Glycan Interaction Resource of the CFGR24GM098791 · NIGMS · EMORY UNIVERSITY · PI CUMMINGS, RICHARD D, PAULSON, JAMES C · 2011 to 2013
$2.6M
Shotgun Glycomics: Linking Glycan Structure and FunctionR01GM085448 · NIGMS · EMORY UNIVERSITY · PI SMITH, DAVID FLETCHER · 2008 to 2011
$2.3M
NCI NIH HHS R01 CA029303NIAID NIH HHS HHSN266200700006CNIGMS NIH HHS GM62116NIGMS NIH HHS P41 GM103694NIGMS NIH HHS R01 GM085448NIGMS NIH HHS R24 GM098791NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Human milk contains a large diversity of free glycans beyond lactose, but their functions are not well understood. To explore their functional recognition, here we describe a shotgun glycan microarray prepared from isolated human milk glycans (HMGs), and our studies on their recognition by viruses, antibodies, and glycan-binding proteins (GBPs), including lectins. The total neutral and sialylated HMGs were derivatized with a bifunctional fluorescent tag, separated by multidimensional HPLC, and archived in a tagged glycan library, which was then used to print a shotgun glycan microarray (SGM). This SGM was first interrogated with well defined GBPs and antibodies. These data demonstrated both the utility of the array and provided preliminary structural information (metadata) about this complex glycome. Anti-TRA-1 antibodies that recognize human pluripotent stem cells specifically recognized several HMGs that were then further structurally defined as novel epitopes for these antibodies. Human influenza viruses and Parvovirus Minute Viruses of Mice also specifically recognized several HMGs. For glycan sequencing, we used a novel approach termed metadata-assisted glycan sequencing (MAGS), in which we combine information from analyses of glycans by mass spectrometry with glycan interactions with defined GBPs and antibodies before and after exoglycosidase treatments on the microarray. Together, these results provide novel insights into diverse recognition functions of HMGs and show the utility of the SGM approach and MAGS as resources for defining novel glycan recognition by GBPs, antibodies, and pathogens.

Indexed as

GlycomicsAnimalsBiomarkersCarbohydrate SequenceCell LineEmbryonic Stem CellsHumansMiceMilk, HumanMolecular Sequence DataPolysaccharidesReceptors, VirusBiomarkersPolysaccharidesReceptors, Virus

Identifiers

PMID23115247
PMCPMC3531791
OpenAlexW2036419366

What OpenQuestion holds

Textmetadata
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.