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Review
. 2001 Oct;69(10):5959-66.
doi: 10.1128/IAI.69.10.5959-5966.2001.

Molecular basis of the intracellular spreading of Shigella

T Suzuki  1 , C Sasakawa
Affiliations
Review

Molecular basis of the intracellular spreading of Shigella

T Suzuki et al. Infect Immun. 2001 Oct.
No abstract available

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Figures

FIG. 1
FIG. 1
Current model for VirG-induced actin polymerization on Shigella in infected mammalian cells. The surface-exposed VirG α-domain recruits vinculin and N-WASP through binding to the glycine-rich repeats of VirG. Vinculin could then interact with actin filaments and VASP which may contribute to actin polymerization (45). The activity of Cdc42 facilitates the formation of the VirG–N-WASP complex, and then the complex could achieve an activating state in which the exposed VCA domain stimulates the Arp2/3 complex to induce rapid actin polymerization. Profilin could promote the actin filament growth by interacting with both N-WASP and monomer actin. PH, plekstrin homology domain; IQ, calmodulin binding domain; GBD, GTPase binding domain that binds Cdc42; PRR, proline-rich region; V, verprolin homology domain; C, cofilin homology domain; A, acidic amino acid segment.
FIG. 2
FIG. 2
Accumulation of the Arp2/3 complex at the actin comet tail of intracellular Shigella (A, B, and C) and Listeria (D, E, and F) in infected HeLa cells. (A and D) The Arp2/3 complex was visualized with fluorescein isothiocyanate-labeled anti-Arp3 antibody. (B and E) Actin filaments were visualized with rhodamine-phalloidin. (C and F) The yellow color in the merged images indicates colocalization between the Arp2/3 complex (green) and actin filaments (red). Arrows indicate an intracellular bacterium forming an actin comet tail. Bar, 10 μm.
FIG. 3
FIG. 3
Electron micrographs of the actin assembly formed by E. coli expressing VirG in Xenopus egg extracts. Actin filaments appear as a dense cross-linked meshwork around the bacterium (A). Actin filaments form a branched network with rigid attachments and a fixed 70° angle between the filaments. The branched points have a globular mass, which would contain the Arp2/3 complex (B). Bars, 500 nm (A) and 100 nm (B).
FIG. 4
FIG. 4
Schematic representations of the components and signaling pathways induced by pathogens for activating the Arp2/3 complex-mediated actin rearrangements. Listeria can stimulate the Arp2/3 complex by direct interaction between the bacterial ActA protein and the Arp2/3 complex. Other pathogens, such as Shigella, EPEC, and vaccinia viruses, exploit their own unique protein to modulate the signaling pathway for inducing a common actin driving system with the N-WASP–Arp2/3 complex.
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