Evidence map›Paper›PMID 25714412›Full record

ArticleAutophagy2015

Binding of the pathogen receptor HSP90AA1 to avibirnavirus VP2 induces autophagy by inactivating the AKT-MTOR pathway.

Boli Hu, Yina Zhang, Lu Jia, Huansheng Wu, Chengfei Fan, Yanting Sun, Chengjin Ye, Min Liao, Jiyong Zhou

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

91 citing papers in PubMed, 144 citations in OpenAlex.

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31 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

9 authors at 2 institutions in 2 countries.

Boli Hua Key Laboratory of Animal Virology of Ministry of Agriculture ; Zhejiang University ; Hangzhou , China.
Yina Zhang
Lu Jia
Huansheng Wu
Chengfei Fan
Yanting Sun
Chengjin Ye
Min Liao
Jiyong Zhou
Zhejiang University · CNNanjing Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is an essential component of host innate and adaptive immunity. Viruses have developed diverse strategies for evading or utilizing autophagy for survival. The response of the autophagy pathways to virus invasion is poorly documented. Here, we report on the induction of autophagy initiated by the pathogen receptor HSP90AA1 (heat shock protein 90 kDa α [cytosolic], class A member 1) via the AKT-MTOR (mechanistic target of rapamycin)-dependent pathway. Transmission electron microscopy and confocal microscopy revealed that intracellular autolysosomes packaged avibirnavirus particles. Autophagy detection showed that early avibirnavirus infection not only increased the amount of light chain 3 (LC3)-II, but also upregulated AKT-MTOR dephosphorylation. HSP90AA1-AKT-MTOR knockdown by RNA interference resulted in inhibition of autophagy during avibirnavirus infection. Virus titer assays further verified that autophagy inhibition, but not induction, enhanced avibirnavirus replication. Subsequently, we found that HSP90AA1 binding to the viral protein VP2 resulted in induction of autophagy and AKT-MTOR pathway inactivation. Collectively, our findings suggest that the cell surface protein HSP90AA1, an avibirnavirus-binding receptor, induces autophagy through the HSP90AA1-AKT-MTOR pathway in early infection. We reveal that upon viral recognition, a direct connection between HSP90AA1 and the AKT-MTOR pathway trigger autophagy, a critical step for controlling infection.

Indexed as

AutophagyAnimalsAvibirnavirusCapsid ProteinsCell MembraneChickensCytosolHEK293 CellsHSP90 Heat-Shock ProteinsHumansLysosomesMicroscopy, ConfocalMicroscopy, Electron, TransmissionMicrotubule-Associated ProteinsPhagosomesPhosphorylationAKT1 protein, humanCapsid ProteinsHSP90AA1 protein, humanHSP90 Heat-Shock ProteinsMAP1LC3A protein, humanMicrotubule-Associated ProteinsMTOR protein, humanProto-Oncogene Proteins c-aktRNA, Small InterferingTOR Serine-Threonine KinasesAKT-MTOR pathwayANOVA, analysis of varianceATG5, autophagy-related 5autophagyavibirnavirusBCA, bicinchoninic acidBECN1, Beclin 1, autophagy-relatedcDNA, complementary DNACoIP, coimmunoprecipitationDMEM, Dulbecco's modified Eagle's mediumdsRNA, double-stranded RNAEBSS, Earle's balanced salt solutioneGFP, enhanced green fluorescent proteinEIF2AK2, eukaryotic translation initiation factor 2-alpha kinase 2EIF2S1, eukaryotic translation initiation factor 2, subunit 1 alphaER, endoplasmic reticulumGAPDH, glyceraldehyde-3-phosphate dehydrogenaseGg, Gallus gallus (chicken)GOPC, golgi-associated PDZ and coiled-coil motif containingGST, glutathione S-transferaseHE-IBDV, heat-inactivated IBDVhpi, hours post-infectionHs, Homo sapiens (human)HSP90AA1HSP90AA1, heat shock protein 90 kDa alpha (cytosolic), class A member 1HSV-1, herpes simplex virus 1IBDV, infectious bursal disease virusIgG, immunoglobulin GLPS, lipopolysaccharidemAb, monoclonal antibodyMAP1LC3/LC3, microtubule-associated protein 1 light chain 3MOI, multiplicity of infectionMTOR, mechanistic target of rapamycin (serine/threonine kinase)Ni-NTA, nickel-nitrilotriacetic acidPAMP, pathogen-associated molecular patternsPBS, phosphate-buffered salinePI3K, phosphoinositide 3-kinasePRR, pattern recognition receptorsRNAi, RNA interferenceSDS, sodium dodecyl sulfateshRNA, short hairpin RNAsiRNA, small interfering RNASQSTM1, sequestosome 1SVP, subviral particleTCID50, 50% tissue culture infectious dosesTLR, toll-like receptorsTSC, tuberous sclerosis complexviral protein VP2VP, viral protein

Identifiers

PMID25714412
PMCPMC4502722
OpenAlexW1545869027

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.