Evidence map›Paper›PMID 30240422›Full record

ArticlePloS one2018

Structural basis of antiviral activity of peptides from MPER of FIV gp36.

Manuela Grimaldi, Ilaria Stillitano, Giuseppina Amodio, Angelo Santoro, Michela Buonocore, Ornella Moltedo, Paolo Remondelli, Anna Maria D'Ursi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 18 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

8 authors at 1 institution in 1 country.

Manuela GrimaldiDepartment of Pharmacy, University of Salerno, Fisciano (SA), Italy.
Ilaria StillitanoDepartment of Pharmacy, University of Salerno, Fisciano (SA), Italy.
Giuseppina AmodioDepartment of Medicine and Surgery, University of Salerno, Baronissi (SA), Italy.
Angelo SantoroDepartment of Pharmacy, University of Salerno, Fisciano (SA), Italy.
Michela BuonocoreDepartment of Pharmacy, University of Salerno, Fisciano (SA), Italy.
Ornella MoltedoDepartment of Pharmacy, University of Salerno, Fisciano (SA), Italy.
Paolo RemondelliDepartment of Medicine and Surgery, University of Salerno, Baronissi (SA), Italy.
Anna Maria D'UrsiDepartment of Pharmacy, University of Salerno, Fisciano (SA), Italy.ORCID 0000-0001-6814-8472
University of Salerno · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Feline immunodeficiency virus (FIV) is a naturally occurring Lentivirus causing acquired immunodeficiency syndrome in felines. It is considered a useful non-primate model to study HIV infection, and to test anti-HIV vaccine. Similarly to HIV, FIV enters cells via a mechanism involving a surface glycoprotein named gp36. C8 is a short synthetic peptide corresponding to the residues 770WEDWVGWI777 of gp36 membrane proximal external region (MPER). It elicits antiviral activity by inhibiting the fusion of the FIV and host cell membrane. C8 is endowed with evident membrane binding property, inducing alteration of the phospholipid bilayer and membrane fusion. The presence and the position of tryptophan residues in C8 are important for antiviral activity: the C8 derivative C6a, obtained by truncating the N-terminal 770WE771 residues, exhibits conserved antiviral activity, while the C8 derivative C6b, derived from the truncation of the C-terminal 776WI777, is nearly inactive. To elucidate the structural factors that induce the different activity profiles of C6a and C6b, in spite of their similarity, we investigated the structural behaviour of the two peptides in membrane mimicking environments. Conformational data on the short peptides C6a and C6b, matched to those of their parent peptide C8, allow describing a pharmacophore model of antiviral fusion inhibitors. This includes the essential structural motifs to design new simplified molecules overcoming the pharmacokinetic and high cost limitations affecting the antiviral entry inhibitors that currently are in therapy.

Indexed as

Amino Acid SequenceAnimalsAntiviral AgentsCatsCircular DichroismDisease Models, AnimalFeline Acquired Immunodeficiency SyndromeGlycoproteinsHIV InfectionsHumansImmunodeficiency Virus, FelineNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein ConformationViral Envelope ProteinsVirus InternalizationAntiviral Agentsenvelope protein, Feline immunodeficiency virusGlycoproteinsPeptide FragmentsViral Envelope Proteins

Identifiers

PMID30240422
PMCPMC6150481
OpenAlexW2890472397

What OpenQuestion 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 OpenQuestion graph.