Evidence map›Paper›PMID 26670246›Full record

ArticleViruses2015

Two Cytoplasmic Acylation Sites and an Adjacent Hydrophobic Residue, but No Other Conserved Amino Acids in the Cytoplasmic Tail of HA from Influenza A Virus Are Crucial for Virus Replication.

Stefanie Siche, Katharina Brett, Lars Möller, Larisa V Kordyukova, Ramil R Mintaev, Andrei V Alexeevski, Michael Veit

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

13 citing papers in PubMed, 24 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

7 authors at 3 institutions in 2 countries.

Stefanie SicheInstitute of Virology, Faculty of Veterinary Medicine, Freie Universität Berlin, 14163 Berlin, Germany. st.siche@googlemail.com.
Katharina BrettInstitute of Virology, Faculty of Veterinary Medicine, Freie Universität Berlin, 14163 Berlin, Germany. katharina.brett@gmail.com.
Lars MöllerRobert Koch Institute, Advanced Light and Electron Microscopy (ZBS4), Nordufer 20, 13353 Berlin, Germany. moellerL@rki.de.
Larisa V KordyukovaA.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia. kord@belozersky.msu.ru.
Ramil R MintaevA.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia. ramil.mintaev@gmail.com.
Andrei V AlexeevskiA.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia. aba@belozersky.msu.ru.
Michael VeitInstitute of Virology, Faculty of Veterinary Medicine, Freie Universität Berlin, 14163 Berlin, Germany. mveit@zedat.fu-berlin.de.
Freie Universität Berlin · DELomonosov Moscow State University · RURobert Koch Institute · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recruitment of the matrix protein M1 to the assembly site of the influenza virus is thought to be mediated by interactions with the cytoplasmic tail of hemagglutinin (HA). Based on a comprehensive sequence comparison of all sequences present in the database, we analyzed the effect of mutating conserved residues in the cytosol-facing part of the transmembrane region and cytoplasmic tail of HA (A/WSN/33 (H1N1) strain) on virus replication and morphology of virions. Removal of the two cytoplasmic acylation sites and substitution of a neighboring isoleucine by glutamine prevented rescue of infectious virions. In contrast, a conservative exchange of the same isoleucine, non-conservative exchanges of glycine and glutamine, deletion of the acylation site at the end of the transmembrane region and shifting it into the tail did not affect virus morphology and had only subtle effects on virus growth and on the incorporation of M1 and Ribo-Nucleoprotein Particles (RNPs). Thus, assuming that essential amino acids are conserved between HA subtypes we suggest that, besides the two cytoplasmic acylation sites (including adjacent hydrophobic residues), no other amino acids in the cytoplasmic tail of HA are indispensable for virus assembly and budding.

Indexed as

Conserved SequenceVirus AssemblyVirus ReleaseVirus ReplicationAcylationAnimalsCell LineDNA Mutational AnalysisDogsHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A Virus, H1N1 SubtypeIsoleucineH1N1 virus hemagglutininHemagglutinin Glycoproteins, Influenza VirusIsoleucineacylationassemblycytoplasmic tailhemagglutinininfluenza virusJ0101M1palmitoylationtransmembrane region

Identifiers

PMID26670246
PMCPMC4690873
OpenAlexW2194233922

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.