The intracellular bacterium Orientia tsutsugamushi hijacks the adaptor protein BICD2 for dynein-based motility
Manigrasso, G.; Saharat, K.; Kullapanich, C.; Boulanger, J.; Morgan, T. E.; Kramer, H.; Salje, J.; Carter, A. P.
Show abstract
The intracellular bacterium Orientia tsutsugamushi relies on the microtubule cytoskeleton and the motor protein dynein to traffic to the perinuclear region within infected cells. However, it remains unclear how the bacterium is coupled to the dynein machinery and how transport is regulated. Here, we discover that O. tsutsugamushi uses its autotransporter protein ScaC to recruit the dynein adaptor BICD2 to the bacterial surface. We show that ScaC is sufficient to engage dynein-based motility in the absence of other bacterial proteins and that BICD2 is required for efficient movement of O. tsutsugamushi during infection. Using TIRF single-molecule assays, we demonstrate that ScaC induces BICD2 to adopt an open conformation which activates the assembly of dynein-dynactin complexes. Our results reveal a novel role for BICD2 during bacterial infection and provide mechanistic insights into the life cycle of an important human pathogen.
Matching journals
The top 3 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- Crystal structure of a guanine nucleotide exchange factor encoded by the scrub typhus pathogen Orientia tsutsugamushi 97%
- Structural basis for autophagy inhibition by the human Rubicon-Rab7 complex 96%
- FETCH enables fluorescent labeling of membrane proteins in vivo with spatiotemporal control in Drosophila 96%
Similar papers in this journal
Similar papers in this journal
- C9orf72-derived arginine-containing dipeptide repeats associate with axonal transport machinery and impede microtubule-based motility 96%
- Phage lysis protein LysM acts as a wedge to block MurJ conformational changes 96%
- Cargo selective vesicle tethering: the structural basis for binding of specific cargo proteins by the Golgi tether component TBC1D23 96%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.