Polar delivery of Legionella type IV secretion system substrates is essential for virulence
Abstract
A recurrent emerging theme is the targeting of proteins to subcellular microdomains within bacterial cells, particularly to the poles. In most cases, it has been assumed that this localization is critical to the protein's function. Legionella pneumophila uses a type IVB secretion system (T4BSS) to export a large number of protein substrates into the cytoplasm of host cells. Here we show that the Legionella export apparatus is localized to the bacterial poles, as is consistent with many T4SS substrates being retained on the phagosomal membrane adjacent to the poles of the bacterium. More significantly, we were able to demonstrate that polar secretion of substrates is critically required for Legionella's alteration of the host endocytic pathway, an activity required for this pathogen's virulence.
Additional Information
© 2017 National Academy of Sciences. Edited by Thomas J. Silhavy, Princeton University, Princeton, NJ, and approved June 1, 2017 (received for review December 30, 2016). Published online before print July 10, 2017. We thank Drs. J. Helbig, R. Isberg, Z. Q. Luo, W. Margolin, and A. L. Sonenshein for providing antibodies; Drs. P. Levin, J. Sexton, and Eep Darwin for helpful discussions; Dr. W. Beatty for the transmission electron microscopy analysis; and Dr. H. Shuman for his valuable suggestion to use a bolA deletion. This work was funded by NIH Grants AI48052 (to J.P.V.) and AI127401 (to G.J.J.). Author contributions: J.P.V. designed research; K.C.J., D.G., and J.P.V. performed research; K.C.J., D.G., Y.-W.C., G.J.J., and J.P.V. analyzed data; and J.P.V. wrote the paper. The authors declare no conflict of interest. This article is a PNAS Direct Submission. This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10.1073/pnas.1621438114/-/DCSupplemental.Attached Files
Published - PNAS-2017-Jeong-8077-82.pdf
Supplemental Material - pnas.1621438114.sm01.mp4
Supplemental Material - pnas.1621438114.sm02.mov
Supplemental Material - pnas.1621438114.sm03.mov
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Additional details
- PMCID
- PMC5544279
- Eprint ID
- 79025
- DOI
- 10.1073/pnas.1621438114
- Resolver ID
- CaltechAUTHORS:20170712-144409863
- NIH
- AI48052
- NIH
- AI127401
- Created
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2017-07-13Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field