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The anti-apoptotic Coxiella burnetii effector protein AnkG is a strain specific virulence factor

2020-09-21Journal article Open access
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dc.contributor.authorSchäfer, Walter
dc.contributor.authorSchmidt, Teresa
dc.contributor.authorCordsmeier, Arne
dc.contributor.authorBorges, Vítor
dc.contributor.authorBeare, Paul A.
dc.contributor.authorPechstein, Julian
dc.contributor.authorSchulze-Luehrmann, Jan
dc.contributor.authorHolzinger, Jonas
dc.contributor.authorWagner, Nicole
dc.contributor.authorBerens, Christian
dc.contributor.authorHeydel, Carsten
dc.contributor.authorGomes, João Paulo
dc.contributor.authorLührmann, Anja
dc.date.accessioned2021-04-02T16:15:55Z
dc.date.available2021-04-02T16:15:55Z
dc.date.issued2020-09-21
dc.description.abstractThe ability to inhibit host cell apoptosis is important for the intracellular replication of the obligate intracellular pathogen Coxiella burnetii, as it allows the completion of the lengthy bacterial replication cycle. Effector proteins injected into the host cell by the C. burnetii type IVB secretion system (T4BSS) are required for the inhibition of host cell apoptosis. AnkG is one of these anti-apoptotic effector proteins. The inhibitory effect of AnkG requires its nuclear localization, which depends on p32-dependent intracellular trafficking and importin-α1-mediated nuclear entry of AnkG. Here, we compared the sequences of ankG from 37 C. burnetii isolates and classified them in three groups based on the predicted protein size. The comparison of the three different groups allowed us to identify the first 28 amino acids as essential and sufficient for the anti-apoptotic activity of AnkG. Importantly, only the full-length protein from the first group is a bona fide effector protein injected into host cells during infection and has anti-apoptotic activity. Finally, using the Galleria mellonella infection model, we observed that AnkG from the first group has the ability to attenuate pathology during in vivo infection, as it allows survival of the larvae despite bacterial replication.pt_PT
dc.description.sponsorshipThis work was supported by the Deutsche Forschungsgemeinschaft (DFG) through the grant LU1357/5-1 to AL. We thank Prof. Robert Heinzen, Dr. Alyssa Ingmundson, Prof. James Samuel and Prof. Thomas Stamminger for providing plasmids, and the Lührmann lab for discussion. Open Access funding provided by Projekt DEAL.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationSci Rep. 2020 Sep 21;10(1):15396. doi: 10.1038/s41598-020-72340-9.pt_PT
dc.identifier.doi10.1038/s41598-020-72340-9pt_PT
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/10400.18/7627
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherNature Researchpt_PT
dc.relation.publisherversionhttps://www.nature.com/articles/s41598-020-72340-9pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAnimalspt_PT
dc.subjectApoptosispt_PT
dc.subjectBacterial Proteinspt_PT
dc.subjectCell Deathpt_PT
dc.subjectCoxiella burnetiipt_PT
dc.subjectHost-Pathogen Interactionspt_PT
dc.subjectHumanspt_PT
dc.subjectProtein Transportpt_PT
dc.subjectSequence Alignmentpt_PT
dc.subjectVirulence Factorspt_PT
dc.subjectInfecções Sistémicas e Zoonosespt_PT
dc.titleThe anti-apoptotic Coxiella burnetii effector protein AnkG is a strain specific virulence factorpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.issue1pt_PT
oaire.citation.startPage15396pt_PT
oaire.citation.titleScientific Reportspt_PT
oaire.citation.volume10pt_PT
rcaap.embargofctAcesso de acordo com política editorial da revista.pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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