Evidence map›Paper›PMID 26138524›Full record

ArticleInnate immunity2015

Arginine-rich histones have strong antiviral activity for influenza A viruses.

Marloes Hoeksema, Shweta Tripathi, Mitchell White, Li Qi, Jeffery Taubenberger, Martin van Eijk, Henk Haagsman, Kevan L Hartshorn

Open access · bronzeAbstract read
In one paragraph

Article in Innate immunity, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

39 citing papers in PubMed, 59 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 3 institutions in 2 countries.

Marloes HoeksemaBoston University School of Medicine, Department of Medicine, Boston MA, USA Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, The Netherlands.
Shweta TripathiBoston University School of Medicine, Department of Medicine, Boston MA, USA.
Mitchell WhiteBoston University School of Medicine, Department of Medicine, Boston MA, USA.
Li QiNational Institute of Allergy and Infectious Diseases, Bethesda MD, USA.
Jeffery TaubenbergerNational Institute of Allergy and Infectious Diseases, Bethesda MD, USA.
Martin van EijkDepartment of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, The Netherlands.
Henk HaagsmanDepartment of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, The Netherlands.
Kevan L HartshornBoston University School of Medicine, Department of Medicine, Boston MA, USA khartsho@bu.edu.
Boston University · USNational Institute of Allergy and Infectious Diseases · USUtrecht University · NL

Funding

Influenza Viral PathogenesisZIAAI000986 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI TAUBENBERGER, JEFFERY · 2009 to 2025
$30.0M
Enhancing Collectin-Mediated Defense Against InfluenzaR01HL069031 · NHLBI · BOSTON MEDICAL CENTER · PI HARTSHORN, KEVAN L · 2002 to 2018
$6.6M
NHLBI NIH HHS R01 HL 069031NHLBI NIH HHS R01 HL069031
6 · The paper itself

Abstract

While histones are best known for DNA binding and transcription-regulating properties, they also have antimicrobial activity against a broad range of potentially pathogenic organisms. Histones are abundant in neutrophil extracellular traps, where they play an important role in NET-mediated antimicrobial killing. Here, we show anti-influenza activity of histones against both seasonal H3N2 and H1N1, but not pandemic H1N1. The arginine rich histones, H3 and H4, had greater neutralizing and viral aggregating activity than the lysine rich histones, H2A and H2B. Of all core histones, histone H4 is most potent in neutralizing IAV, and incubation with IAV with histone H4 results in a decrease in uptake and viral replication by epithelial cells when measured by qRT-PCR. The antiviral activity of histone H4 is mediated principally by direct effects on viral particles. Histone H4 binds to IAV as assessed by ELISA and co-sedimentation of H4 with IAV. H4 also induces aggregation, as assessed by confocal microscopy and light transmission assays. Despite strong antiviral activity against the seasonal IAV strains, H4 was inactive against pandemic H1N1. These findings indicate a possible role for histones in the innate immune response against IAV.

Indexed as

Antiviral AgentsArginineCell LineEpithelial CellsHistonesHumansImmunity, InnateInfluenza A virusInfluenza, HumanProtein BindingVirus InternalizationVirus ReplicationAntiviral AgentsArginineHistonesantimicrobial peptideHistonesinfluenzainnate immunitypandemic

Identifiers

PMID26138524
PMCPMC5431080
OpenAlexW1902742304

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.