Evidence map›Paper›PMID 27892522›Full record

ArticleScientific reports2016

SARS-CoV fusion peptides induce membrane surface ordering and curvature.

Luis G M Basso, Eduardo F Vicente, Edson Crusca, Eduardo M Cilli, Antonio J Costa-Filho

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

40 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Article
  3. The Interplay of Lipids and Peptides in Membrane Merger.Advances in experimental medicine and biology · 2026
    Review
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  13. Role of Surface Tension in Microrobot Penetration in Membranes.... International Conference on Manipulation Automation and Robotics at Small Scales (MARSS). International Conference on Manipulation Automation and Robotics at Small Scales · 2022
    Article
  14. Review
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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

5 authors at 2 institutions in 1 country.

Luis G M BassoGrupo de Biofísica Molecular Sérgio Mascarenhas, Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Trabalhador São-carlense, 400, Centro, São Carlos, SP, Brazil.
Eduardo F VicenteFaculdade de Ciências e Engenharia, UNESP - Univ Estadual Paulista, Campus de Tupã. Rua Domingos da Costa Lopes, 780, 17602-496, Tupã, SP, Brazil.
Edson CruscaDepartamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista. Rua Prof. Franscisco Degni, 55, 14800-900, Araraquara, SP, Brazil.
Eduardo M CilliDepartamento de Bioquímica e Tecnologia Química, Instituto de Química, UNESP - Univ Estadual Paulista. Rua Prof. Franscisco Degni, 55, 14800-900, Araraquara, SP, Brazil.
Antonio J Costa-FilhoLaboratório de Biofísica Molecular, Departamento de Física, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. Av. Bandeirantes, 3900, 14040-901, Ribeirão Preto, SP, Brazil.
Universidade Estadual Paulista (Unesp) · BRUniversidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viral membrane fusion is an orchestrated process triggered by membrane-anchored viral fusion glycoproteins. The S2 subunit of the spike glycoprotein from severe acute respiratory syndrome (SARS) coronavirus (CoV) contains internal domains called fusion peptides (FP) that play essential roles in virus entry. Although membrane fusion has been broadly studied, there are still major gaps in the molecular details of lipid rearrangements in the bilayer during fusion peptide-membrane interactions. Here we employed differential scanning calorimetry (DSC) and electron spin resonance (ESR) to gather information on the membrane fusion mechanism promoted by two putative SARS FPs. DSC data showed the peptides strongly perturb the structural integrity of anionic vesicles and support the hypothesis that the peptides generate opposing curvature stresses on phosphatidylethanolamine membranes. ESR showed that both FPs increase lipid packing and head group ordering as well as reduce the intramembrane water content for anionic membranes. Therefore, bending moment in the bilayer could be generated, promoting negative curvature. The significance of the ordering effect, membrane dehydration, changes in the curvature properties and the possible role of negatively charged phospholipids in helping to overcome the high kinetic barrier involved in the different stages of the SARS-CoV-mediated membrane fusion are discussed.

Indexed as

Membrane FusionVirus InternalizationCalorimetry, Differential ScanningCell MembraneElectron Spin Resonance SpectroscopyPeptidesSevere acute respiratory syndrome-related coronavirusThermodynamicsViral Fusion ProteinsPeptidesViral Fusion Proteins

Identifiers

PMID27892522
PMCPMC5125003
OpenAlexW2559296654

What OpenQuestion holds

Textmetadata
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.