Evidence map›Paper›PMID 22993149›Full record

ArticleJournal of virology2012

Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pretriggered state.

Matteo Porotto, Zuhair W Salah, Long Gui, Ilaria DeVito, Eric M Jurgens, Hong Lu, Christine C Yokoyama, Laura M Palermo, Kelly K Lee, Anne Moscona

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  11. Isolation and Molecular Characterisation of Respirovirus 3 in Wild Boar.Animals : an open access journal from MDPI · 2023
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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

10 authors at 2 institutions in 2 countries.

Matteo PorottoDepartment of Pediatrics, Weill Medical College of Cornell University, New York, New York, USA. map2028@med.cornell.edu
Zuhair W Salah
Long Gui
Ilaria DeVito
Eric M Jurgens
Hong Lu
Christine C Yokoyama
Laura M Palermo
Kelly K Lee
Anne Moscona
Cornell University · USUniversity of Washington · US

Funding

Molecular basis for paramyxovirus entryR01AI031971 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOSCONA, ANNE · 1998 to 2016
$6.6M
Waters ACQUITY UPLC M-Class with NanoLockSpray ionization sourceR01GM099989 · NIGMS · UNIVERSITY OF WASHINGTON · PI LEE, KELLY KEISEN · 2012 to 2020
$3.5M
NIAID NIH HHS 3R01AI031971-19S1NIAID NIH HHS R01 AI031971NIAID NIH HHS R01AI31971NIGMS NIH HHS R01 GM099989NIGMS NIH HHS R01-GM099989
6 · The paper itself

Abstract

The hemagglutinin (HA)-neuraminidase protein (HN) of paramyxoviruses carries out three discrete activities, each of which affects the ability of HN to promote viral fusion and entry: receptor binding, receptor cleaving (neuraminidase), and triggering of the fusion protein. Binding of HN to its sialic acid receptor on a target cell triggers its activation of the fusion protein (F), which then inserts into the target cell and mediates the membrane fusion that initiates infection. We provide new evidence for a fourth function of HN: stabilization of the F protein in its pretriggered state before activation. Influenza virus hemagglutinin protein (uncleaved HA) was used as a nonspecific binding protein to tether F-expressing cells to target cells, and heat was used to activate F, indicating that the prefusion state of F can be triggered to initiate structural rearrangement and fusion by temperature. HN expression along with uncleaved HA and F enhances the F activation if HN is permitted to engage the receptor. However, if HN is prevented from engaging the receptor by the use of a small compound, temperature-induced F activation is curtailed. The results indicate that HN helps stabilize the prefusion state of F, and analysis of a stalk domain mutant HN reveals that the stalk domain of HN mediates the F-stabilization effect.

Indexed as

Virus Internalizationbeta-GalactosidaseCell LineFlow CytometryHN ProteinHumansMicroscopy, FluorescenceParainfluenza Virus 1, HumanProtein StabilityReceptors, Cell SurfaceTemperatureViral Fusion Proteinsbeta-GalactosidaseHN ProteinReceptors, Cell Surfacesialic acid receptorViral Fusion Proteins

Identifiers

PMID22993149
PMCPMC3497673
OpenAlexW2165442038

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.