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Legionella effector AnkX interacts with host nuclear protein PLEKHN1
Xiaobo Yu1, Rebecca R Noll2, Barbara P Romero Dueñas2
1State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences-Beijing (PHOENIX Center), Beijing Institute of Radiation Medicine, Beijing, 102206, China.
BMC Microbiology
|February 14, 2018
Summary
Legionella pneumophila effector AnkX targets nuclear proteins, including PLEKHN1, and may manipulate host inflammatory responses. This discovery expands understanding of bacterial pathogenesis and host-pathogen interactions.
Area of Science:
- Microbiology
- Cell Biology
- Immunology
Background:
- Legionella pneumophila causes Legionnaires' disease by proliferating in macrophages.
- The pathogen evades lysosomal fusion using effector proteins like AnkX.
- AnkX's host interactions and functions are not fully understood.
Purpose of the Study:
- Investigate the protein interaction network of AnkX.
- Identify novel host proteins interacting with AnkX.
- Elucidate AnkX's role in host cell manipulation.
Main Methods:
- Utilized nucleic acid programmable protein array (NAPPA) for high-throughput screening.
- Confirmed interactions using in vitro pull-down and co-immunoprecipitation assays.
- Employed structured illumination microscopy for co-localization studies.
Main Results:
- Discovered PLEKHN1 as a novel AnkX interaction partner.
- Confirmed AnkX-PLEKHN1 interaction via multiple assays.
- Observed AnkX co-localization with PLEKHN1 on vesicular compartments and identified AnkX's ankyrin repeat region interaction.
Conclusions:
- AnkX targets nuclear host proteins beyond Rab GTPases.
- PLEKHN1 associates with inflammatory response proteins.
- AnkX may possess novel functions in modulating host inflammatory responses.
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