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© Research
Publication : FEBS letters

Deciphering the specific interaction between the acyl carrier protein IacP and the T3SS-major hydrophobic translocator SipB from Salmonella.

Team: Stress Adaptation and Metabolism (SAMe)
Member: Emmanuelle Bouveret
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 01 Jan 2020

Canestrari MJ, Serrano B, Bartoli J, Prima V, Bornet O, Puppo R, Bouveret E, Guerlesquin F, Viala JP,

Link to Pubmed [PMID] – 31486064

Link to DOI – 10.1002/1873-3468.13593

FEBS Lett 2020 01; 594(2): 251-265

Salmonella is a facultative intracellular pathogen that invades epithelial cells of the intestine using the SPI-1 Type 3 secretion System (T3SS). Insertion of the SPI-1 T3SS translocon is facilitated by acylation of the translocator SipB, which involves a protein-protein interaction with the acyl carrier protein IacP. Using nuclear magnetic resonance and biological tests, we identified the residues of IacP that are involved in the interaction with SipB. Our results suggest that the 4′-phosphopantetheine group that functionalizes IacP participates in the interaction. Its solvent exposition may rely on two residues highly conserved in acyl carrier proteins associated with T3SS. This study is the first to address the specificity of acyl carrier proteins associated with T3SS.