Evidence map›Paper›PMID 34254825›Full record

ArticlemSystems2021

RNA-Protein Interaction Analysis of SARS-CoV-2 5' and 3' Untranslated Regions Reveals a Role of Lysosome-Associated Membrane Protein-2a during Viral Infection.

Rohit Verma, Sandhini Saha, Shiv Kumar, Shailendra Mani, Tushar Kanti Maiti, Milan Surjit

Open access · goldAbstract read
In one paragraph

Article in mSystems, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

  1. Pooled it
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  17. Ribosome biogenesis in disease: new players and therapeutic targets.Signal transduction and targeted therapy · 2023
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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 2 institutions in 1 country.

Rohit Verma *Virology Laboratory, Translational Health Science and Technology Institutegrid.464764.3, NCR Biotech Science Cluster, Faridabad, Haryana, India.
Sandhini Saha *Laboratory of Functional Proteomics, Regional Centre for Biotechnology, NCR Biotech Science Cluster, Faridabad, Haryana, India.
Shiv KumarVirology Laboratory, Translational Health Science and Technology Institutegrid.464764.3, NCR Biotech Science Cluster, Faridabad, Haryana, India.
Shailendra ManiTranslational Health Science and Technology Institutegrid.464764.3, NCR Biotech Science Cluster, Faridabad, Haryana, India.
Tushar Kanti MaitiLaboratory of Functional Proteomics, Regional Centre for Biotechnology, NCR Biotech Science Cluster, Faridabad, Haryana, India.
Milan SurjitVirology Laboratory, Translational Health Science and Technology Institutegrid.464764.3, NCR Biotech Science Cluster, Faridabad, Haryana, India.
Translational Health Science and Technology Institute · INRegional Centre for Biotechnology · IN

Funding

DST | Science and Engineering Research Board (SERB) IPA/2020/000233
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a positive-strand RNA virus. The viral genome is capped at the 5' end, followed by an untranslated region (UTR). There is a poly(A) tail at the 3' end, preceded by a UTR. The self-interaction between the RNA regulatory elements present within the 5' and 3' UTRs and their interaction with host/virus-encoded proteins mediate the function of the 5' and 3' UTRs. Using an RNA-protein interaction detection (RaPID) assay coupled to liquid chromatography with tandem mass spectrometry, we identified host interaction partners of SARS-CoV-2 5' and 3' UTRs and generated an RNA-protein interaction network. By combining these data with the previously known protein-protein interaction data proposed to be involved in virus replication, we generated the RNA-protein-protein interaction (RPPI) network, likely to be essential for controlling SARS-CoV-2 replication. Notably, bioinformatics analysis of the RPPI network revealed the enrichment of factors involved in translation initiation and RNA metabolism. Lysosome-associated membrane protein-2a (Lamp2a), the receptor for chaperone-mediated autophagy, is one of the host proteins that interact with the 5' UTR. Further studies showed that the Lamp2 level is upregulated in SARS-CoV-2-infected cells and that the absence of the Lamp2a isoform enhanced the viral RNA level whereas its overexpression significantly reduced the viral RNA level. Lamp2a and viral RNA colocalize in the infected cells, and there is an increased autophagic flux in infected cells, although there is no change in the formation of autophagolysosomes. In summary, our study provides a useful resource of SARS-CoV-2 5' and 3' UTR binding proteins and reveals the role of Lamp2a protein during SARS-CoV-2 infection.

Indexed as

3′ UTR5′ UTRcoronavirusLamp2Lamp2aRNA-protein interaction networkSARS-CoV-2virus-host interaction

Identifiers

PMID34254825
PMCPMC8407388
OpenAlexW3181708537

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.