Evidence map›Paper›PMID 25157143›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Efficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain.

Melinda A Brindley, Philippe Plattet, Richard Karl Plemper

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 17 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

3 authors at 2 institutions in 2 countries.

Melinda A BrindleyInstitute for Biomedical Sciences, Georgia State University, Atlanta, GA 30303; and.
Philippe PlattetNeurovirology Unit, Division of Experimental Clinical Research, Veterinary Public Health, Vetsuisse Faculty, University of Bern, CH-3012 Bern, Switzerland.
Richard Karl PlemperInstitute for Biomedical Sciences, Georgia State University, Atlanta, GA 30303; and rplemper@gsu.edu.
Georgia State University · USUniversity of Bern · CH

Funding

Identification and Pre-Clinical Evaluation of Measles Virus InhibitorsR01AI071002 · NIAID · GEORGIA STATE UNIVERSITY · PI PLEMPER, RICHARD K. · 2006 to 2022
$6.6M
Cryo-Electron and Biochemical Anaysis of Native Paramyxovirus Fusion ComplexesR01AI083402 · NIAID · GEORGIA STATE UNIVERSITY · PI PLEMPER, RICHARD K. · 2011 to 2015
$1.7M
Cryo-Electron and Biochemical Analysis of Native Paramyxovirus Fusion ComplexesR56AI083402 · NIAID · EMORY UNIVERSITY · PI PLEMPER, RICHARD K. · 2010 to 2010
$380k
NIAID NIH HHS AI071002NIAID NIH HHS AI083402NIAID NIH HHS R01 AI071002NIAID NIH HHS R01 AI083402NIAID NIH HHS R56 AI083402
6 · The paper itself

Abstract

Enveloped viruses such as HIV and members of the paramyxovirus family use metastable, proteinaceous fusion machineries to merge the viral envelope with cellular membranes for infection. A hallmark of the fusogenic glycoproteins of these pathogens is refolding into a thermodynamically highly stable fusion core structure composed of six antiparallel α-helices, and this structure is considered instrumental for pore opening and/or enlargement. Using a paramyxovirus fusion (F) protein, we tested this paradigm by engineering covalently restricted F proteins that are predicted to be unable to close the six-helix bundle core structure fully. Several candidate bonds formed efficiently, resulting in F trimers and higher-order complexes containing covalently linked dimers. The engineered F complexes were incorporated into recombinant virions efficiently and were capable of refolding into a postfusion conformation without temporary or permanent disruption of the disulfide bonds. They efficiently formed fusion pores based on virus replication and quantitative cell-to-cell and virus-to-cell fusion assays. Complementation of these F mutants with a monomeric, fusion-inactive F variant enriched the F oligomers for heterotrimers containing a single disulfide bond, without affecting fusion complementation profiles compared with standard F protein. Our demonstration that complete closure of the fusion core does not drive paramyxovirus entry may aid the design of strategies for inhibiting virus entry.

Indexed as

Virus ReplicationAmino Acid SequenceAnimalsChickensChlorocebus aethiopsCOS CellsCysteineDisulfidesHumansKineticsMeasles virusModels, MolecularMolecular Sequence DataMutant ProteinsProtein EngineeringProtein MultimerizationCysteineDisulfidesMutant ProteinsViral Fusion Proteinsmeasles virusmembrane fusion

Identifiers

PMID25157143
PMCPMC4246953
OpenAlexW2077580500

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.