Evidence map›Paper›PMID 34325286›Full record

ArticleVirology2021

SARS-CoV-2 and other coronaviruses bind to phosphorylated glycans from the human lung.

Lauren Byrd-Leotis, Yi Lasanajak, Thomas Bowen, Kelly Baker, Xuezheng Song, Mehul S Suthar, Richard D Cummings, David A Steinhauer

Open access · greenAbstract read
In one paragraph

Article in Virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

8 citing papers in PubMed, 16 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

8 authors at 2 institutions in 1 country.

Lauren Byrd-LeotisDepartment of Microbiology and Immunology, Emory University School of Medicine Atlanta, GA, 30322, USA; Centers for Excellence in Influenza Research and Surveillance, Emory-UGA CEIRS, Atlanta, GA, 30322, USA. Electronic address: labyrd@emory.edu.
Yi LasanajakDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Thomas BowenDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Kelly BakerBeth Israel Deaconess Medical Center, Department of Surgery and Harvard Medical School Center for Glycoscience, Harvard Medical School, Boston, MA, 02115, USA.
Xuezheng SongDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Mehul S SutharDepartment of Pediatrics, Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA, 30322, USA.
Richard D CummingsBeth Israel Deaconess Medical Center, Department of Surgery and Harvard Medical School Center for Glycoscience, Harvard Medical School, Boston, MA, 02115, USA; Centers for Excellence in Influenza Research and Surveillance, Emory-UGA CEIRS, Atlanta, GA, 30322, USA.
David A SteinhauerDepartment of Microbiology and Immunology, Emory University School of Medicine Atlanta, GA, 30322, USA; Centers for Excellence in Influenza Research and Surveillance, Emory-UGA CEIRS, Atlanta, GA, 30322, USA.
Emory University · USBeth Israel Deaconess Medical Center · US

Funding

Overall Priority Score P41GM103694 · NIGMS · EMORY UNIVERSITY · PI CUMMINGS, RICHARD D · 2013 to 2018
$6.9M
Protein-Glycan Interaction Resource at the National Center for Functional Glycomics (NCFG)R24GM137763 · NIGMS · BETH ISRAEL DEACONESS MEDICAL CENTER · PI RICHARD D CUMMINGS · 2020 to 2026
$5.8M
NIAID NIH HHS HHSN272201400004CNIGMS NIH HHS P41 GM103694NIGMS NIH HHS R24 GM137763
6 · The paper itself

Abstract

SARS-CoV, MERS-CoV, and potentially SARS-CoV-2 emerged as novel human coronaviruses following cross-species transmission from animal hosts. Although the receptor binding characteristics of human coronaviruses are well documented, the role of carbohydrate binding in addition to recognition of proteinaceous receptors has not been fully explored. Using natural glycan microarray technology, we identified N-glycans in the human lung that are recognized by various human and animal coronaviruses. All viruses tested, including SARS-CoV-2, bound strongly to a range of phosphorylated, high mannose N-glycans and to a very specific set of sialylated structures. Examination of two linked strains, human CoV OC43 and bovine CoV Mebus, reveals shared binding to the sialic acid form Neu5Gc (not found in humans), supporting the evidence for cross-species transmission of the bovine strain. Our findings, revealing robust recognition of lung glycans, suggest that these receptors could play a role in the initial stages of coronavirus attachment and entry.

Indexed as

AnimalsCattleCOVID-19Host Microbial InteractionsHumansLungMannoseMiddle East Respiratory Syndrome CoronavirusN-Acetylneuraminic AcidPhosphorylationPolysaccharidesProtein Array AnalysisProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusMannoseN-Acetylneuraminic AcidPolysaccharidesSpike Glycoprotein, CoronavirusCoronavirus receptorsGlycan receptorsHuman lung glycan microarrayPhosphorylated glycansSARS-CoV-2

Identifiers

PMID34325286
PMCPMC8299723
OpenAlexW3183460526

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.