Evidence map›Paper›PMID 25062117›Full record

ArticleThe Biochemical journal2014

Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism.

Safder S Ganaie, Absarul Haque, Erdong Cheng, Tania S Bonny, Nilshad N Salim, Mohammad A Mir

Abstract read
In one paragraph

Article in The Biochemical 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
1.6field-weighted citation impact, top 16% 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, 24 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

6 authors at 1 institution in 1 country.

Safder S Ganaie*Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, U.S.A.
Absarul Haque*Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, U.S.A.
Erdong Cheng*Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, U.S.A.
Tania S Bonny*Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, U.S.A.
Nilshad N Salim*Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, U.S.A.
Mohammad A Mir*Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, U.S.A.
University of Kansas Medical Center · US

Funding

Novel Approaches for the Control of Microbial PathogensP30GM103326 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI LUTKENHAUS, JOSEPH F · 2012 to 2016
$5.3M
Identification and characterization of inhibitors for hantavirus replicationR01AI095236 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI MIR, MOHAMMAD A · 2011 to 2013
$1.1M
Characterization of hantavirus N protein-mediated translation mechanismR21AI097355 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI MIR, MOHAMMAD A · 2012 to 2013
$415k
NIAID NIH HHS 1R21 AI097355-01NIAID NIH HHS R01 AI095236NIAID NIH HHS R01AI095236-01NIAID NIH HHS R21 AI097355NIGMS NIH HHS P30 GM103326
6 · The paper itself

Abstract

The hantaviral zoonotic diseases pose a significant threat to human health due to the lack of potential antiviral therapeutics or a vaccine against hantaviruses. N (Sin Nombre hantavirus nucleocapsid protein) augments mRNA translation. N binds to both the mRNA 5' cap and 40S ribosomal subunit via RPS19 (ribosomal protein S19). N with the assistance of the viral mRNA 5'-UTR preferentially favours the translation of a downstream ORF. We identified and characterized the RPS19-binding domain at the N-terminus of N. Its deletion did not influence the secondary structure, but affected the conformation of trimeric N molecules. The N variant lacking the RPS19-binding region was able to bind both the mRNA 5' cap and panhandle-like structure, formed by the termini of viral genomic RNA. In addition, the N variant formed stable trimers similar to wild-type N. Use of this variant in multiple experiments provided insights into the mechanism of ribosome loading during N-mediated translation strategy. The present study suggests that N molecules individually associated with the mRNA 5' cap and RPS19 of the 40S ribosomal subunit undergo N-N interaction to facilitate the engagement of N-associated ribosomes at the mRNA 5' cap. This has revealed new targets for therapeutic intervention of hantavirus infection.

Indexed as

Amino Acid SequenceBinding SitesHeLa CellsHumansMolecular Sequence DataNucleocapsid ProteinsOrthohantavirusPeptide Chain Initiation, TranslationalRibosomal ProteinsNucleocapsid ProteinsRibosomal Proteinsribosomal protein S19

Identifiers

PMID25062117
PMCPMC4315616
OpenAlexW2330496614

What OpenQuestion holds

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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.