Evidence map›Paper›PMID 24988208›Full record

ArticlePloS one2014

Alzheimer's associated β-amyloid protein inhibits influenza A virus and modulates viral interactions with phagocytes.

Mitchell R White, Ruth Kandel, Shweta Tripathi, David Condon, Li Qi, Jeffrey Taubenberger, Kevan L Hartshorn

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed, 2 pooled it
6.2field-weighted citation impact, top 3% 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

114 citing papers in PubMed, 2 syntheses or guidelines pooled it, 191 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Accumulation of amyloid beta in human glioblastomas.Clinical and experimental immunology · 2020
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54 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 1 country.

Mitchell R WhiteDepartment of Medicine, Boston University School of Medicine, Boston, Massachusetts, United States of America.
Ruth KandelHebrew Senior Life, Harvard Medical School, Boston, Massachusetts, United States of America.
Shweta TripathiDepartment of Medicine, Boston University School of Medicine, Boston, Massachusetts, United States of America.
David CondonDepartment of Medicine, Boston University School of Medicine, Boston, Massachusetts, United States of America.
Li QiNational Institute of Allergy and Infectious Disease, Bethesda, Maryland, United States of America.
Jeffrey TaubenbergerNational Institute of Allergy and Infectious Disease, Bethesda, Maryland, United States of America.
Kevan L HartshornDepartment of Medicine, Boston University School of Medicine, Boston, Massachusetts, United States of America.
Boston University · USNational Institute of Allergy and Infectious Diseases · USHarvard University · US

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
Collectins and Innate Defense against Inhaled PathogensP01AI083222 · NIAID · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SEATON, BARBARA A · 2009 to 2010
$4.9M
Intramural NIH HHSNHLBI NIH HHS HL 069031NHLBI NIH HHS R01 HL069031NIAID NIH HHS AI-83222NIAID NIH HHS P01 AI083222
6 · The paper itself

Abstract

Accumulation of β-Amyloid (βA) is a key pathogenetic factor in Alzheimer's disease; however, the normal function of βA is unknown. Recent studies have shown that βA can inhibit growth of bacteria and fungi. In this paper we show that βA also inhibits replication of seasonal and pandemic strains of H3N2 and H1N1 influenza A virus (IAV) in vitro. The 42 amino acid fragment of βA (βA42) had greater activity than the 40 amino acid fragment. Direct incubation of the virus with βA42 was needed to achieve optimal inhibition. Using quantitative PCR assays βA42 was shown to reduce viral uptake by epithelial cells after 45 minutes and to reduce supernatant virus at 24 hours post infection. βA42 caused aggregation of IAV particles as detected by light transmission assays and electron and confocal microscopy. βA42 did not stimulate neutrophil H2O2 production or extracellular trap formation on its own, but it increased both responses stimulated by IAV. In addition, βA42 increased uptake of IAV by neutrophils. βA42 reduced viral protein synthesis in monocytes and reduced IAV-induced interleukin-6 production by these cells. Hence, we demonstrate for the first time that βA has antiviral activity and modulates viral interactions with phagocytes.

Indexed as

Host-Pathogen InteractionsAmyloid beta-PeptidesAnimalsAntiviral AgentsCell LineHumansInfluenza A virusInfluenza A Virus, H1N1 SubtypeInfluenza A Virus, H3N2 SubtypeInfluenza, HumanMonocytesNeutrophilsOrthomyxoviridae InfectionsPeptide FragmentsPhagocytesAmyloid beta-Peptidesamyloid beta-protein (1-42)Antiviral AgentsPeptide Fragments

Identifiers

PMID24988208
PMCPMC4079246
OpenAlexW2164223927

What OpenQuestion holds

Textmetadata
LicenceCC0
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.