Evidence map›Paper›PMID 38704431›Full record

ArticleScientific reports2024

An Elastin-like Polypeptide-fusion peptide targeting capsid-tegument interface as an antiviral against cytomegalovirus infection.

Komal Beeton, Dipanwita Mitra, Adesanya A Akinleye, John A Howell, Christian S Yu, Gene L Bidwell, Ritesh Tandon

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. Article
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.

Komal BeetonDepartment of Cell and Molecular Biology, Center for Immunology and Microbial Research, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS, 39216, USA.
Dipanwita MitraDepartment of Cell and Molecular Biology, Center for Immunology and Microbial Research, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS, 39216, USA.
Adesanya A AkinleyeDepartment of Pharmacology and Toxicology, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS, 39216, USA.
John A HowellDepartment of Neurology, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS, 39216, USA.
Christian S YuDepartment of Cell and Molecular Biology, Center for Immunology and Microbial Research, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS, 39216, USA.
Gene L BidwellDepartment of Cell and Molecular Biology, Center for Immunology and Microbial Research, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS, 39216, USA.
Ritesh TandonDepartment of Cell and Molecular Biology, Center for Immunology and Microbial Research, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS, 39216, USA. ritesh.tandon@nih.gov.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tegument protein pp150 of Human Cytomegalovirus (HCMV) is known to be essential for the final stages of virus maturation and mediates its functions by interacting with capsid proteins. Our laboratory has previously identified the critical regions in pp150 important for pp150-capsid interactions and designed peptides similar in sequence to these regions, with a goal to competitively inhibit capsid maturation. Treatment with a specific peptide (PepCR2 or P10) targeted to pp150 conserved region 2 led to a significant reduction in murine CMV (MCMV) growth in cell culture, paving the way for in vivo testing in a mouse model of CMV infection. However, the general pharmacokinetic parameters of peptides, including rapid degradation and limited tissue and cell membrane permeability, pose a challenge to their successful use in vivo. Therefore, we designed a biopolymer-stabilized elastin-like polypeptide (ELP) fusion construct (ELP-P10) to enhance the bioavailability of P10. Antiviral efficacy and cytotoxic effects of ELP-P10 were studied in cell culture, and pharmacokinetics, biodistribution, and antiviral efficacy were studied in a mouse model of CMV infection. ELP-P10 maintained significant antiviral activity in cell culture, and this conjugation significantly enhanced P10 bioavailability in mouse tissues. The fluorescently labeled ELP-P10 accumulated to higher levels in mouse liver and kidneys as compared to the unconjugated P10. Moreover, viral titers from vital organs of MCMV-infected mice indicated a significant reduction of virus load upon ELP-P10 treatment. Therefore, ELP-P10 has the potential to be developed into an effective antiviral against CMV infection.

Indexed as

Antiviral AgentsCytomegalovirus InfectionsElastinMuromegalovirusPeptidesPhosphoproteinsViral Matrix ProteinsAnimalsCapsidCapsid ProteinsCytomegalovirusDisease Models, AnimalElastin-Like PolypeptidesMiceRecombinant Fusion ProteinsAntiviral AgentsCapsid ProteinsElastinElastin-Like PolypeptidesPeptidesPhosphoproteinspp150 protein, CytomegalovirusRecombinant Fusion ProteinsViral Matrix Proteins

Identifiers

PMID38704431
PMCPMC11069587

What Socratic holds

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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 Socratic graph.