Evidence map›Paper›PMID 33635872›Full record

ArticlePloS one2021

Histone H4 potentiates neutrophil inflammatory responses to influenza A virus: Down-modulation by H4 binding to C-reactive protein and Surfactant protein D.

I-Ni Hsieh, Mitchell White, Marloes Hoeksema, Xavier Deluna, Kevan Hartshorn

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. The role of extracellular histones in COVID-19.Journal of internal medicine · 2023
    Review
  7. Article
  8. Review
  9. 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

5 authors at 2 institutions in 2 countries.

I-Ni HsiehDepartment of Medicine, Section of Hematology Oncology, Boston University School of Medicine, Boston, Massachusetts, United States of America.
Mitchell WhiteDepartment of Medicine, Section of Hematology Oncology, Boston University School of Medicine, Boston, Massachusetts, United States of America.
Marloes HoeksemaUniversity of Amsterdam, Amsterdam, Netherlands.
Xavier DelunaDepartment of Medicine, Section of Hematology Oncology, Boston University School of Medicine, Boston, Massachusetts, United States of America.
Kevan HartshornDepartment of Medicine, Section of Hematology Oncology, Boston University School of Medicine, Boston, Massachusetts, United States of America.ORCID 0000-0002-7196-7433
Boston University · USAmsterdam University of the Arts · NL

Funding

Enhancing Collectin-Mediated Defense Against InfluenzaR01HL069031 · NHLBI · BOSTON MEDICAL CENTER · PI HARTSHORN, KEVAN L · 2002 to 2018
$6.6M
QUANTSTUDIO 12K FLEX OPEN ARRAY REAL-TIME PCR SYSTEMS10OD023663 · OD · BOSTON MEDICAL CENTER · PI DENG, LINGYI L · 2017 to 2017
$186k
NHLBI NIH HHS R01 HL069031NIH HHS S10 OD023663
6 · The paper itself

Abstract

Neutrophils participate in the early phase of the innate response to uncomplicated influenza A virus (IAV) infection but also are a major component in later stages of severe IAV or COVID 19 infection where neutrophil extracellular traps (NETs) and associated cell free histones are highly pro-inflammatory. It is likely that IAV interacts with histones during infection. We show that histone H4 binds to IAV and aggregates viral particles. In addition, histone H4 markedly potentiates IAV induced neutrophil respiratory burst responses. Prior studies have shown reactive oxidants to be detrimental during severe IAV infection. C reactive protein (CRP) and surfactant protein D (SP-D) rise during IAV infection. We now show that both of these innate immune proteins bind to histone H4 and significantly down regulate respiratory burst and other responses to histone H4. Isolated constructs composed only of the neck and carbohydrate recognition domain of SP-D also bind to histone H4 and partially limit neutrophil responses to it. These studies indicate that complexes formed of histones and IAV are a potent neutrophil activating stimulus. This finding could account for excess inflammation during IAV or other severe viral infections. The ability of CRP and SP-D to bind to histone H4 may be part of a protective response against excessive inflammation in vivo.

Indexed as

Cells, CulturedC-Reactive ProteinHistonesHumansImmunity, InnateInflammationInfluenza A virusInfluenza A Virus, H1N1 SubtypeInfluenza A Virus, H3N2 SubtypeInfluenza, HumanNeutrophilsPulmonary Surfactant-Associated Protein DC-Reactive ProteinHistonesPulmonary Surfactant-Associated Protein D

Identifiers

PMID33635872
PMCPMC7909658
OpenAlexW3132832555

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.