Oxysterol-binding protein (OSBP) enhances replication of intracellular Salmonella and binds the Salmonella SPI-2 effector SseL via its N-terminus

Effectors translocated into the host cell by Salmonella enterica serovar Typhimurium are critical for bacterial virulence. For many effectors, the mechanisms of their interactions with host pathways are not yet understood. We have recently found an interaction between the SPI-2 effector SseL and oxy...

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Bibliographic Details
Published in:Microbes and infection 2012-02, Vol.14 (2), p.148-154
Main Authors: Auweter, Sigrid D., Yu, Hong B., Arena, Ellen T., Guttman, Julian A., Finlay, B. Brett
Format: Article
Language:English
Subjects:
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Cell Line
DNA, Complementary - genetics
Endopeptidases - genetics
Endopeptidases - metabolism
Epithelial Cells - microbiology
Female
Fundamental and applied biological sciences. Psychology
HeLa Cells
Host-Pathogen Interactions
Humans
Intracellular Space - microbiology
Membrane Proteins - metabolism
Microbiology
Miscellaneous
OSBP
Oxysterol-binding protein
Protein Binding
Protein Interaction Mapping
Protein Structure, Tertiary
Protein Transport
Receptors, Steroid - metabolism
Salmonella enterica serovar Typhimurium
Salmonella Infections - microbiology
Salmonella typhimurium - pathogenicity
Salmonella typhimurium - physiology
SPI-2
SseL
Type three secretion
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Summary:Effectors translocated into the host cell by Salmonella enterica serovar Typhimurium are critical for bacterial virulence. For many effectors, the mechanisms of their interactions with host pathways are not yet understood. We have recently found an interaction between the SPI-2 effector SseL and oxysterol-binding protein (OSBP). We show here that SseL binds the N-terminus of OSBP and that S. Typhimurium infection results in redistribution of OSBP. We furthermore demonstrate that OSBP is required for efficient replication of intracellular S. Typhimurium. This suggests that S. Typhimurium hijacks OSBP-dependent pathways to benefit its intracellular life-style, possibly by SseL- and OSBP-mediated manipulation of host lipid metabolism.
ISSN:1286-4579
1769-714X
DOI:10.1016/j.micinf.2011.09.003