Evidence map›Paper›PMID 38880069›Full record

ArticleVirology2024

Receptor binding and immunogenic properties of the receptor binding domain of influenza D virus hemagglutinin-esterase-fusion protein expressed from Escherichia coli.

Ahsan Naveed, Jieshi Yu, Steven Lawson, Rongyuan Gao, Shuisong Ni, Mousumi Paulchakrabarti, Biswa Choudhury, Jane Christopher-Hennings, Eric Nelson, Zizhang Sheng and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. 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.

Ahsan NaveedMaxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY, 40546, USA.
Jieshi YuMaxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY, 40546, USA.
Steven LawsonDepartment of Veterinary and Biomedical Science, South Dakota State University, Brookings, SD, 57007, USA.
Rongyuan GaoDepartment of Biology and Microbiology, South Dakota State University, Brookings, SD, 57007, USA.
Shuisong NiDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA.
Mousumi PaulchakrabartiDepartment of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, CA, 92093, USA.
Biswa ChoudhuryDepartment of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, CA, 92093, USA.
Jane Christopher-HenningsDepartment of Veterinary and Biomedical Science, South Dakota State University, Brookings, SD, 57007, USA.
Eric NelsonDepartment of Veterinary and Biomedical Science, South Dakota State University, Brookings, SD, 57007, USA.
Zizhang ShengZuckerman Mind Brian Behavior Institute, Columbia University, New York, NY, USA.
Michael A KennedyDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA.
Feng LiMaxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY, 40546, USA. Electronic address: Feng.Li@uky.edu.
Dan WangMaxwell H. Gluck Equine Research Center, Department of Veterinary Science, University of Kentucky, Lexington, KY, 40546, USA. Electronic address: Dan.Wang@uky.edu.

Funding

Influenza D Virus Entry and Tissue TropismR01AI141889 · NIAID · UNIVERSITY OF KENTUCKY · PI LI, FENG · 2018 to 2022
$2.6M
NIAID NIH HHS R01 AI141889
6 · The paper itself

Abstract

The hemagglutinin-esterase-fusion (HEF) protein binds 9-O-acetylated sialic acids-containing glycans on the cell surface and drives influenza D virus (IDV) entry. The HEF is a primary determinant of the exceptional thermal and acid stability observed in IDV infection biology. Here, we expressed and purified the receptor binding domain (RBD) of the IDV HEF protein in Escherichia coli and characterized its receptor binding and antigenic properties. The data from these experiments indicate that (i) the RBD can bind with specificity to turkey red blood cells (RBC), and its binding can be specifically inhibited by IDV antibody; (ii) the RBD efficiently binds to the cell surface of MDCK cells expressing the receptor of IDV; and (iii) anti-RBD antibodies are capable of blocking RBD attachment to MDCK cells as well as of inhibiting the virus from agglutinating RBCs. These observations support the utility of this RBD in future receptor and entry studies of IDV.

Indexed as

ErythrocytesEscherichia coliProtein BindingReceptors, VirusAnimalsAntibodies, ViralDeltainfluenzavirusDogsGene ExpressionHemagglutinins, ViralHumansMadin Darby Canine Kidney CellsProtein DomainsViral Fusion ProteinsAntibodies, Viralhemagglutinin esteraseHemagglutinins, ViralReceptors, VirusViral Fusion ProteinsBovine influenzaHemagglutinin-esterase-fusion proteinReceptor binding domainType D

Identifiers

PMID38880069
PMCPMC11257787

What OpenQuestion holds

Textmetadata
LicenceTDM
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.