Evidence map›Paper›PMID 29056462›Full record

ArticleJournal of molecular biology2017

The SARS-CoV Fusion Peptide Forms an Extended Bipartite Fusion Platform that Perturbs Membrane Order in a Calcium-Dependent Manner.

Alex L Lai, Jean K Millet, Susan Daniel, Jack H Freed, Gary R Whittaker

Abstract read
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed, 3 pooled it
7.4field-weighted citation impact, top 2% 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

118 citing papers in PubMed, 3 syntheses or guidelines pooled it, 224 citations in OpenAlex.

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58 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Alex L LaiDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, United States.
Jean K MilletDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, United States.
Susan DanielSchool of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853, United States.
Jack H FreedDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, United States.
Gary R WhittakerDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, United States. Electronic address: gary.whittaker@cornell.edu.
Cornell University · US

Funding

TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
ELECTRON SPIN RELAXATION IN MODEL MEMBRANESR01EB003150 · NIBIB · CORNELL UNIVERSITY ITHACA · PI FREED, JACK H · 2005 to 2016
$4.9M
Electron Spin Relaxation in Model MembranesR01GM123779 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2017 to 2020
$2.1M
Spike protein cleavage-activation and emergence of coronaviruses with extended trR21AI111085 · NIAID · CORNELL UNIVERSITY · PI WHITTAKER, GARY R · 2014 to 2015
$419k
NIAID NIH HHS R21 AI111085NIBIB NIH HHS R01 EB003150NIGMS NIH HHS P41 GM103521NIGMS NIH HHS R01 GM123779
6 · The paper itself

Abstract

Coronaviruses (CoVs) are a major infectious disease threat and include the pathogenic human pathogens of zoonotic origin: severe acute respiratory syndrome CoV (SARS-CoV) and Middle East respiratory syndrome CoV (MERS-CoV). Entry of CoVs into host cells is mediated by the viral spike (S) protein, which is structurally categorized as a class I viral fusion protein, within the same group as influenza virus and HIV. However, S proteins have two distinct cleavage sites that can be activated by a much wider range of proteases. The exact location of the CoV fusion peptide (FP) has been disputed. However, most evidence suggests that the domain immediately downstream of the S2' cleavage site is the FP (amino acids 798-818 SFIEDLLFNKVTLADAGFMKQY for SARS-CoV, FP1). In our previous electron spin resonance spectroscopic studies, the membrane-ordering effect of influenza virus, HIV, and Dengue virus FPs has been consistently observed. In this study, we used this effect as a criterion to identify and characterize the bona fide SARS-CoV FP. Our results indicate that both FP1 and the region immediately downstream (amino acids 816-835 KQYGECLGDINARDLICAQKF, FP2) induce significant membrane ordering. Furthermore, their effects are calcium dependent, which is consistent with in vivo data showing that calcium is required for SARS-CoV S-mediated fusion. Isothermal titration calorimetry showed a direct interaction between calcium cations and both FPs. This Ca

Indexed as

Amino Acid SequenceBase SequenceCalciumHEK293 CellsHumansMembrane FusionPeptide FragmentsProtein ConformationSequence HomologySevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusVirus InternalizationCalciumPeptide FragmentsSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVcoronaviruselectron spin resonancemembrane fusionspike glycoproteinviral entry

Identifiers

PMID29056462
PMCPMC5705393
OpenAlexW2766494877

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.