Evidence map›Paper›PMID 32641475›Full record

ArticleJournal of virology2020

H9N2 Influenza Virus Infections in Human Cells Require a Balance between Neuraminidase Sialidase Activity and Hemagglutinin Receptor Affinity.

Yasuha Arai, Emad Mohamed Elgendy, Tomo Daidoji, Madiha Salah Ibrahim, Takao Ono, Nongluk Sriwilaijaroen, Yasuo Suzuki, Takaaki Nakaya, Kazuhiko Matsumoto, Yohei Watanabe

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 27 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

10 authors at 6 institutions in 3 countries.

Yasuha AraiDepartment of Infectious Diseases, Graduate School of Medical Sciences, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Emad Mohamed ElgendyDepartment of Infectious Diseases, Graduate School of Medical Sciences, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Tomo DaidojiDepartment of Infectious Diseases, Graduate School of Medical Sciences, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Madiha Salah IbrahimDepartment of Microbiology and Immunology, Faculty of Veterinary Medicine, Damanhour University, Damanhour, Egypt.
Takao OnoThe Institute of Scientific and Industrial Research, Osaka University, Osaka, Japan.
Nongluk SriwilaijaroenDepartment of Preclinical Sciences, Faculty of Medicine, Thammasat University, Pathumthani, Thailand.
Yasuo SuzukiSchool of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.
Takaaki NakayaDepartment of Infectious Diseases, Graduate School of Medical Sciences, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Kazuhiko MatsumotoThe Institute of Scientific and Industrial Research, Osaka University, Osaka, Japan.
Yohei WatanabeDepartment of Infectious Diseases, Graduate School of Medical Sciences, Kyoto Prefectural University of Medicine, Kyoto, Japan nabe@koto.kpu-m.ac.jp.
Kyoto Prefectural University of Medicine · JPChubu University · JPDamanhour University · EGOsaka Research Institute of Industrial Science and Technology · JPOsaka University · JPThammasat University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Some avian influenza (AI) viruses have a deletion of up to 20 to 30 amino acids in their neuraminidase (NA) stalk. This has been associated with changes in virus replication and host range. Currently prevalent H9N2 AI viruses have only a 2- or 3-amino-acid deletion, and such deletions were detected in G1 and Y280 lineage viruses, respectively. The effect of an NA deletion on the H9N2 phenotype has not been fully elucidated. In this study, we isolated G1 mutants that carried an 8-amino-acid deletion in their NA stalk. To systematically analyze the effect of NA stalk length and concomitant (de)glycosylation on G1 replication and host range, we generated G1 viruses that had various NA stalk lengths and that were either glycosylated or not glycosylated. The stalk length was correlated with NA sialidase activity, using low-molecular-weight substrates, and with virus elution efficacy from erythrocytes. G1 virus replication in avian cells and eggs was positively correlated with the NA stalk length but was negatively correlated in human cells and mice. NA stalk length modulated G1 virus entry into host cells, with shorter stalks enabling more efficient G1 entry into human cells. However, with a hemagglutinin (HA) with a higher α2,6-linked sialylglycan affinity, the effect of NA stalk length on G1 virus infection was reversed, with shorter NA stalks reducing virus entry into human cells. These results indicate that a balance between HA binding affinity and NA sialidase activity, modulated by NA stalk length, is required for optimal G1 virus entry into human airway cells.

Indexed as

Gene Expression Regulation, ViralAmino Acid SequenceAnimalsChickensGenotypeGlycosylationHemagglutinin Glycoproteins, Influenza VirusHemagglutininsHost-Pathogen InteractionsHost SpecificityHumansInfluenza A Virus, H9N2 SubtypeInfluenza in BirdsMiceNeuraminidaseOrthomyxoviridae Infectionshemagglutinin, avian influenza A virusHemagglutinin Glycoproteins, Influenza VirusHemagglutininsNeuraminidaseReceptors, Virusfunctional balanceH9N2 influenza virushemagglutininhost rangeinfectionneuraminidase stalk

Identifiers

PMID32641475
PMCPMC7459563
OpenAlexW3040182809

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.