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Periplasmic protein EipA determines envelope stress resistance and virulence in Brucella abortus

Julien Herrou, Jonathan W. Willett, Aretha Fiebig, Lydia M. Varesio, Daniel M. Czyż, Jason X. Cheng, Eveline Ultee, Ariane Briegel, Lance Bigelow, Gyorgy Babnigg, Youngchang Kim, View ORCID ProfileSean Crosson
doi: https://doi.org/10.1101/442541
Julien Herrou
aDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA
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Jonathan W. Willett
aDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA
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Aretha Fiebig
aDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA
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Lydia M. Varesio
aDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA
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Daniel M. Czyż
bDepartment of Microbiology and Cell Science, University of Florida, Gainesville, Florida, USA
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Jason X. Cheng
cDepartment of Pathology, The University of Chicago, Chicago, Illinois, USA
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Eveline Ultee
dDepartment of Biology, Universiteit Leiden, Leiden, Netherlands
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Ariane Briegel
dDepartment of Biology, Universiteit Leiden, Leiden, Netherlands
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Lance Bigelow
eBiosciences Division, Argonne National Laboratory, Argonne, Illinois, USA
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Gyorgy Babnigg
eBiosciences Division, Argonne National Laboratory, Argonne, Illinois, USA
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Youngchang Kim
eBiosciences Division, Argonne National Laboratory, Argonne, Illinois, USA
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Sean Crosson
aDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA
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  • ORCID record for Sean Crosson
  • For correspondence: scrosson@uchicago.edu
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Summary

Molecular components of the Brucella abortus cell envelope play a major role in its ability to infect, colonize and survive inside mammalian host cells. In this study, we have defined a role for a conserved gene of unknown function in B. abortus envelope stress resistance and infection. Expression of this gene, which we name eipA, is directly activated by the essential cell cycle regulator, CtrA. eipA encodes a soluble periplasmic protein that adopts an unusual eight-stranded β-barrel fold. Deletion of eipA attenuates replication and survival in macrophage and mouse infection models, and results in sensitivity to treatments that compromise the integrity of the cell envelope. Transposon disruption of genes required for LPS O-polysaccharide biosynthesis is synthetically lethal with eipA deletion. This genetic connection between O-polysaccharide and eipA is corroborated by our discovery that eipA is essential in Brucella ovis, a naturally rough species that harbors mutations in several genes required for O-polysaccharide production. Conditional depletion of eipA expression in B. ovis results in a cell chaining phenotype, providing evidence that eipA directly or indirectly influences cell division in Brucella. We conclude that EipA is a molecular determinant of Brucella virulence that functions to maintain cell envelope integrity and influences cell division.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted November 20, 2018.
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Periplasmic protein EipA determines envelope stress resistance and virulence in Brucella abortus
Julien Herrou, Jonathan W. Willett, Aretha Fiebig, Lydia M. Varesio, Daniel M. Czyż, Jason X. Cheng, Eveline Ultee, Ariane Briegel, Lance Bigelow, Gyorgy Babnigg, Youngchang Kim, Sean Crosson
bioRxiv 442541; doi: https://doi.org/10.1101/442541
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Periplasmic protein EipA determines envelope stress resistance and virulence in Brucella abortus
Julien Herrou, Jonathan W. Willett, Aretha Fiebig, Lydia M. Varesio, Daniel M. Czyż, Jason X. Cheng, Eveline Ultee, Ariane Briegel, Lance Bigelow, Gyorgy Babnigg, Youngchang Kim, Sean Crosson
bioRxiv 442541; doi: https://doi.org/10.1101/442541

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