Evidence map›Paper›PMID 24978308›Full record

ArticleBiochemical and biophysical research communications2014

Inhibition of influenza virus infection and hemagglutinin cleavage by the protease inhibitor HAI-2.

Brian S Hamilton, Changik Chung, Soreen Y Cyphers, Vera D Rinaldi, Valerie C Marcano, Gary R Whittaker

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

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  5. Human coronavirus HKU1 recognition of the TMPRSS2 host receptor.bioRxiv : the preprint server for biology · 2024
    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

6 authors at 1 institution in 1 country.

Brian S HamiltonDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.
Changik ChungDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.
Soreen Y CyphersDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.
Vera D RinaldiDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.
Valerie C MarcanoDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.
Gary R WhittakerDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA. Electronic address: grw7@cornell.edu.
Cornell University · US

Funding

Endocytosis of Influenza VirusesR01AI048678 · NIAID · CORNELL UNIVERSITY ITHACA · PI WHITTAKER, GARY R · 2001 to 2011
$3.4M
NIAID NIH HHS HHSN266200700008CNIAID NIH HHS R01 AI048678NIAID NIH HHS R01 AI48678
6 · The paper itself

Abstract

Influenza virus remains a significant concern to public health, with the continued potential for a high fatality pandemic. Vaccination and antiviral therapeutics are effective measures to circumvent influenza virus infection, however, multiple strains have emerged that are resistant to the antiviral therapeutics currently on the market. With this considered, investigation of alternative antiviral therapeutics is being conducted. One such approach is to inhibit cleavage activation of the influenza virus hemagglutinin (HA), which is an essential step in the viral replication cycle that permits viral-endosome fusion. Therefore, targeting trypsin-like, host proteases responsible for HA cleavage in vivo may prove to be an effective therapeutic. Hepatocyte growth factor activator inhibitor 2 (HAI-2) is naturally expressed in the respiratory tract and is a potent inhibitor of trypsin-like serine proteases, some of which have been determined to cleave HA. In this study, we demonstrate that HAI-2 is an effective inhibitor of cleavage of HA from the human-adapted H1 and H3 subtypes. HAI-2 inhibited influenza virus H1N1 infection in cell culture, and HAI-2 administration showed protection in a mouse model of influenza. HAI-2 has the potential to be an effective, alternative antiviral therapeutic for influenza.

Indexed as

AnimalsAntiviral AgentsDogsFemaleHEK293 CellsHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A Virus, H1N1 SubtypeInfluenza A Virus, H3N2 SubtypeMadin Darby Canine Kidney CellsMembrane ProteinsMice, Inbred BALB CMolecular MimicryOligopeptidesOrthomyxoviridae InfectionsRecombinant ProteinsAntiviral AgentsHemagglutinin Glycoproteins, Influenza Virushemagglutinin, human influenza A virusMembrane ProteinsOligopeptidesRecombinant ProteinsSpint2 protein, mouseHAI-2HemagglutininInfluenza virusProtease inhibitor

Identifiers

PMID24978308
PMCPMC4465281
OpenAlexW2053662779

What OpenQuestion holds

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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.