Evidence map›Paper›PMID 33712145›Full record

ArticleCarbohydrate polymers2021

Heparan sulfates from bat and human lung and their binding to the spike protein of SARS-CoV-2 virus.

Lufeng Yan, Yuefan Song, Ke Xia, Peng He, Fuming Zhang, Shiguo Chen, Robert Pouliot, Daniel J Weiss, Ritesh Tandon, John T Bates and 5 more

Open access · greenAbstract read
In one paragraph

Article in Carbohydrate polymers, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

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  11. Is heparan sulfate a target for inhibition of RNA virus infection?American journal of physiology. Cell physiology · 2022
    Review
  12. Article
  13. Safety and Pharmacokinetics of Intranasally Administered Heparin.medRxiv : the preprint server for health sciences · 2022
    Article
  14. Review
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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

15 authors at 5 institutions in 2 countries.

Lufeng YanCollege of Biosystems Engineering and Food Science, National-Local Joint Engineering Laboratory of Intelligent Food Technology and Equipment, Zhejiang University, Hangzhou, 310058, China; Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, United States.
Yuefan SongDepartment of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, United States.
Ke XiaDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, United States.
Peng HeDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, United States.
Fuming ZhangDepartment of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, United States.
Shiguo ChenCollege of Biosystems Engineering and Food Science, National-Local Joint Engineering Laboratory of Intelligent Food Technology and Equipment, Zhejiang University, Hangzhou, 310058, China.
Robert PouliotLarner College of Medicine, University of Vermont, Burlington, VT, United States.
Daniel J WeissLarner College of Medicine, University of Vermont, Burlington, VT, United States.
Ritesh TandonDepartment of Microbiology and Immunology, University of Mississippi Medical Center, Jackson, MS, 39216, United States.
John T BatesDepartment of Microbiology and Immunology, University of Mississippi Medical Center, Jackson, MS, 39216, United States.
Dallas R EdererDepartment of Microbiology and Immunology, University of Mississippi Medical Center, Jackson, MS, 39216, United States.
Dipanwita MitraDepartment of Microbiology and Immunology, University of Mississippi Medical Center, Jackson, MS, 39216, United States.
Poonam SharmaDepartment of Microbiology and Immunology, University of Mississippi Medical Center, Jackson, MS, 39216, United States.
April DavisRabies Laboratory, New York State Department of Health Wadsworth Center, Albany, New York, United States.
Robert J LinhardtDepartment of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, United States; Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, United States. Electronic address: linhar@rpi.edu.
Rensselaer Polytechnic Institute · USUniversity of Mississippi Medical Center · USUniversity of Vermont · USNew York State Department of Health · USZhejiang University · CN

Funding

The role ofglycosaminoglycan N-sulfation in glomerular biology/pathobiologyR01DK111958 · NIDDK · LOUISIANA STATE UNIV HSC SHREVEPORT · PI MCCARTHY, KEVIN JOHN · 2017 to 2021
$2.6M
An Automated Platform for the CE-MS Analysis of GlycosaminoglycansU01CA231074 · NCI · UNIVERSITY OF GEORGIA · PI AMSTER, I JONATHAN · 2018 to 2020
$895k
NCI NIH HHS U01 CA231074NIDDK NIH HHS R01 DK111958
6 · The paper itself

Abstract

Severe acute respiratory syndrome-related coronavirus-2 (SARS-CoV-2) has resulted in a pandemic and continues to spread at an unprecedented rate around the world. Although a vaccine has recently been approved, there are currently few effective therapeutics to fight its associated disease in humans, COVID-19. SARS-CoV-2 and the related severe acute respiratory syndrome (SARS-CoV-1), and Middle East respiratory syndrome (MERS-CoV) result from zoonotic respiratory viruses that have bats as the primary host and an as yet unknown secondary host. While each of these viruses has different protein-based cell-surface receptors, each rely on the glycosaminoglycan, heparan sulfate as a co-receptor. In this study we compare, for the first time, differences and similarities in the structure of heparan sulfate in human and bat lungs. Furthermore, we show that the spike glycoprotein of COVID-19 binds 3.5 times stronger to human lung heparan sulfate than bat lung heparan sulfate.

Indexed as

AnimalsChiropteraFemaleHeparan SulfateHumansLungMaleMolecular StructureMolecular WeightProtein BindingReceptors, VirusSARS-CoV-2Spike Glycoprotein, CoronavirusHeparan SulfateReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Disaccharide compositionHeparan sulfateMolecular weightSARS-CoV-2 virusSpike protein RBD

Identifiers

PMID33712145
PMCPMC7882221
OpenAlexW3129787752

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.