Publications by authors named "Hiromu Oide"
The bacterium Legionella pneumophila secretes numerous effector proteins that manipulate endoplasmic reticulum (ER)-derived vesicles to form the Legionella-containing vacuole (LCV). Despite extensive studies, whether the LCV membrane is separate from or connected to the host ER network remains unclear. Here, we show that the smooth ER (sER) is closely associated with the LCV early in infection.
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- Rab GTPases are targeted by bacterial pathogens to manipulate membrane trafficking, with specific focus on Rab10's role during infection.
- The study identifies ubiquitin signaling, particularly from SidE and SidC ligases, as essential for the modification and recruitment of Rab10 to bacterial vacuoles.
- MavC functions as a negative regulator, crosslinking ubiquitin to SdcB and inhibiting its action, which leads to the removal of Rab10 from vacuoles during later infection stages.
Article Synopsis
- The bacterium uses its Dot/Icm secretion system to inject about 330 effector proteins into host cells, forming a structure called the LCV.
- Research shows that during early infection, the LCV closely interacts with the smooth endoplasmic reticulum (sER), but over time, it develops into a unique membrane distinct from the host's endoplasmic reticulum (ER).
- The protein BAP31 helps facilitate this transition by acting as a bridge between the sER and rough ER (rER), while a newly identified effector, Lpg1152, is crucial for recruiting BAP31 to assist this transformation.