Evidence map›Paper›PMID 31315988›Full record

ArticleJournal of virology2019

Biochemical Analysis of Coronavirus Spike Glycoprotein Conformational Intermediates during Membrane Fusion.

Miyuki Kawase, Michiyo Kataoka, Kazuya Shirato, Shutoku Matsuyama

Abstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

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  8. Prothrombotic Phenotype in COVID-19: Focus on Platelets.International journal of molecular sciences · 2021
    Review
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  15. Computational and structural biotechnology journal · 2021
    Article
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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

4 authors at 1 institution in 1 country.

Miyuki KawaseDepartment of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan.
Michiyo KataokaDepartment of Pathology, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan.
Kazuya ShiratoDepartment of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan.
Shutoku MatsuyamaDepartment of Virology III, Murayama Branch, National Institute of Infectious Diseases, Tokyo, Japan matuyama@nih.go.jp.
National Institute of Infectious Diseases · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A fusion protein expressed on the surface of enveloped viruses mediates fusion of the viral and cellular membranes to facilitate virus infection. Pre- and postfusion structures of viral fusion proteins have been characterized, but conformational changes between them remain poorly understood. Here, we examined the intermediate conformation of the murine coronavirus fusion protein, called the spike protein, which must be cleaved by a cellular protease following receptor binding. Western blot analysis of protease digestion products revealed that two subunits (67 and 69 kDa) are produced from a single spike protein (180 kDa). These two subunits were considered to be by-products derived from conformational changes and were useful for probing the intermediate conformation of the spike protein. Interaction with a heptad repeat (HR) peptide revealed that these subunits adopt packed and unpacked conformations, respectively, and two-dimensional electrophoresis revealed a trimeric assembly. Based on biochemical observations, we propose an asymmetric trimer model for the intermediate structure of the spike protein. Receptor binding induces the membrane-binding potential of the trimer, in which at least one HR motif forms a packed-hairpin structure, while membrane fusion subunits are covered by the receptor-binding subunit, thereby preventing the spike protein from forming the typical homotrimeric prehairpin structure predicted by the current model of class I viral fusion protein. Subsequent proteolysis induces simultaneous packing of the remaining unpacked HRs upon assembly of three HRs at the central axis to generate a six-helix bundle. Our model proposes a key mechanism for membrane fusion of enveloped viruses.

Indexed as

Virus InternalizationAnimalsCryoelectron MicroscopyMiceMolecular WeightMurine hepatitis virusProtein ConformationProtein MultimerizationProtein SubunitsProteolysisSpike Glycoprotein, CoronavirusProtein SubunitsSpike Glycoprotein, Coronavirusconformational changecoronavirusintermediatemembrane fusionspikeWestern blotting

Identifiers

PMID31315988
PMCPMC6744234
OpenAlexW2957711193

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.