TY  - JOUR
ID  - discovery76177
UR  - https://doi.org/10.1016/j.chom.2007.02.001
VL  - 1
A1  - Brawn, LC
A1  - Hayward, RD
A1  - Koronakis, V
EP  - 75
N2  - Salmonellae employ two type III secretion systems (T3SSs), SPI1 and SPI2, to deliver virulence effectors into mammalian cells. SPI1 effectors, including actin-binding SipA, trigger initial bacterial uptake, whereas SPI2 effectors promote subsequent replication within customized Salmonella-containing vacuoles (SCVs). SCVs sequester actin filaments and subvert microtubule-dependent motors to migrate to the perinuclear region. We demonstrate that SipA delivery continues after Salmonella internalization, with dosage being restricted by host-mediated degradation. SipA is exposed on the cytoplasmic face of the SCV, from where it stimulates bacterial replication in both nonphagocytic cells and macrophages. Although SipA is sufficient to target and redistribute late endosomes, during infection it cooperates with the SPI2 effector SifA to modulate SCV morphology and ensure perinuclear positioning. Our findings define an unexpected additional function for SipA postentry and reveal precise intracellular communication between effectors deployed by distinct T3SSs underlying SCV biogenesis.
TI  - Salmonella SPI1 effector SipA persists after entry and cooperates with a SPI2 effector to regulate phagosome maturation and intracellular replication
Y1  - 2007/03/15/
N1  - This article is available under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/3.0/).
KW  - Actins
KW  -  Animals
KW  -  Bacterial Proteins
KW  -  Cell Nucleus
KW  -  Endosomes
KW  -  Genomic Islands
KW  -  HeLa Cells
KW  -  Humans
KW  -  Kinesin
KW  -  Membrane Proteins
KW  -  Mice
KW  -  Microfilament Proteins
KW  -  Microtubule-Organizing Center
KW  -  NIH 3T3 Cells
KW  -  Phagosomes
KW  -  Recombinant Fusion Proteins
KW  -  Salmonella typhimurium
IS  - 1
JF  - Cell Host & Microbe
AV  - public
SN  - 1934-6069
SP  - 63
ER  -