Evidence map›Paper›PMID 33378104›Full record

ArticleChemMedChem2021

Exploring Viral Interference Using Peptides: Molecular Determinants of HIV-1 Inhibition by a Peptide Derived from Human Pegivirus-1 Envelope Protein E2.

Rebecca Hoffmann, Tamara Ruegamer, Johanna Schaubächer, Anette Rohrhofer, Peter Kirmeß, Karen M Fiebig, Barbara Schmidt, Jutta Eichler

Open access · hybridAbstract read
In one paragraph

Article in ChemMedChem, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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

8 authors at 3 institutions in 1 country.

Rebecca HoffmannDepartment of Chemistry and Pharmacy, University of Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058, Erlangen, Germany.
Tamara RuegamerInstitute of Clinical Microbiology and Hygiene, University of Regensburg, Franz-Josef-Strauß-Allee 11, 93053, Regensburg, Germany.
Johanna SchaubächerInstitute of Medical Microbiology and Hygiene, University of Regensburg, Franz-Josef-Strauß-Allee 11, 93053, Regensburg, Germany.
Anette RohrhoferInstitute of Clinical Microbiology and Hygiene, University of Regensburg, Franz-Josef-Strauß-Allee 11, 93053, Regensburg, Germany.
Peter KirmeßDepartment of Chemistry and Pharmacy, University of Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058, Erlangen, Germany.
Karen M FiebigDepartment of Chemistry and Pharmacy, University of Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058, Erlangen, Germany.
Barbara SchmidtInstitute of Clinical Microbiology and Hygiene, University of Regensburg, Franz-Josef-Strauß-Allee 11, 93053, Regensburg, Germany.ORCID 0000-0003-0059-0349
Jutta EichlerDepartment of Chemistry and Pharmacy, University of Erlangen-Nürnberg, Nikolaus-Fiebiger-Str. 10, 91058, Erlangen, Germany.ORCID 0000-0001-6683-9456
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEInstitute of Medical Microbiology and Hygiene · DEUniversity of Regensburg · DE

Funding

German Research FoundationReForM A program of the Faculty of Medicine, University of Regensburg GRK 1910
6 · The paper itself

Abstract

Co-infection with the human pegivirus 1 (HPgV-1) often has a beneficial effect on disease progression in HIV-1-infected individuals. Several HPgV-1 proteins and peptides, including a 20-mer peptide (P6-2) derived from the N-terminal region of the HPgV-1 surface protein E2, have been associated with this phenomenon, which is referred to as viral interference. We identified the cysteine residues, the hydrophobic core tetrapeptide, as well as the C-terminal negative charge as key factors for the HIV-1 inhibitory activity of P6-2. Analysis of mutations in P6-2-resistant HIV-1 indicated a binding site for the peptide in the HIV-1 envelope glycoprotein gp120. In fact, P6-2 was shown to bind to soluble gp120, as well as to a peptide presenting the gp120 V3 loop. Furthermore, the HIV-1 inhibitory activity of P6-2 could be revoked by the V3 loop peptide, thus indicating a molecular mechanism that involves interaction of P6-2 with the gp120 V3 loop.

Indexed as

Amino Acid SequenceBinding SitesGB virus CHIV-1HIV Envelope Protein gp120MutationPeptide FragmentsProtein BindingViral InterferenceViral Proteinsgp120 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120Peptide FragmentsViral Proteinsgp120 V3 loopHIV-1human pegiviruspeptidesviral interference

Identifiers

PMID33378104
PMCPMC8248410
OpenAlexW3115055901

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.