Evidence map›Paper›PMID 25547032›Full record

ArticleVirology journal2014

Identification of putative interactions between swine and human influenza A virus nucleoprotein and human host proteins.

Alex Generous, Molly Thorson, Jeff Barcus, Joseph Jacher, Marc Busch, Heidi Sleister

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Host metabolic responses to SARS-CoV-2 and influenza viruses: parallels and contrasts.Metabolomics : Official journal of the Metabolomic Society · 2026
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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.

Alex GenerousBiology Department, Drake University, 1344 27th St., Des Moines, IA, 50311, USA. generous.alex@mayo.edu.
Molly ThorsonBiology Department, Drake University, 1344 27th St., Des Moines, IA, 50311, USA. mttho@umich.edu.
Jeff BarcusBiology Department, Drake University, 1344 27th St., Des Moines, IA, 50311, USA. barcu010@umn.edu.
Joseph JacherBiology Department, Drake University, 1344 27th St., Des Moines, IA, 50311, USA. joejacher@gmail.com.
Marc BuschBiology Department, Drake University, 1344 27th St., Des Moines, IA, 50311, USA. marc.busch@drake.edu.
Heidi SleisterBiology Department, Drake University, 1344 27th St., Des Moines, IA, 50311, USA. heidi.sleister@drake.edu.
Drake University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundInfluenza A viruses (IAVs) are important pathogens that affect the health of humans and many additional animal species. IAVs are enveloped, negative single-stranded RNA viruses whose genome encodes at least ten proteins. The IAV nucleoprotein (NP) is a structural protein that associates with the viral RNA and is essential for virus replication. Understanding how IAVs interact with host proteins is essential for elucidating all of the required processes for viral replication, restrictions in species host range, and potential targets for antiviral therapies.

methodsIn this study, the NP from a swine IAV was cloned into a yeast two-hybrid "bait" vector for expression of a yeast Gal4 binding domain (BD)-NP fusion protein. This "bait" was used to screen a Y2H human HeLa cell "prey" library which consisted of human proteins fused to the Gal4 protein's activation domain (AD). The interaction of "bait" and "prey" proteins resulted in activation of reporter genes.

resultsSeventeen positive bait-prey interactions were isolated in yeast. All of the "prey" isolated also interact in yeast with a NP "bait" cloned from a human IAV strain. Isolation and sequence analysis of the cDNAs encoding the human prey proteins revealed ten different human proteins. These host proteins are involved in various host cell processes and structures, including purine biosynthesis (PAICS), metabolism (ACOT13), proteasome (PA28B), DNA-binding (MSANTD3), cytoskeleton (CKAP5), potassium channel formation (KCTD9), zinc transporter function (SLC30A9), Na+/K+ ATPase function (ATP1B1), and RNA splicing (TRA2B).

conclusionsTen human proteins were identified as interacting with IAV NP in a Y2H screen. Some of these human proteins were reported in previous screens aimed at elucidating host proteins relevant to specific viral life cycle processes such as replication. This study extends previous findings by suggesting a mechanism by which these host proteins associate with the IAV, i.e., physical interaction with NP. Furthermore, this study revealed novel host protein-NP interactions in yeast.

Indexed as

Host-Pathogen InteractionsProtein Interaction MappingAlphainfluenzavirusAnimalsGenes, ReporterHeLa CellsHumansNucleocapsid ProteinsRNA-Binding ProteinsSwineTwo-Hybrid System TechniquesViral Core ProteinsNP protein, Influenza A virusNucleocapsid ProteinsRNA-Binding ProteinsViral Core Proteins

Identifiers

PMID25547032
PMCPMC4297426
OpenAlexW2120020485

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.