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Review
. 2000 Feb 21;191(4):587-92.
doi: 10.1084/jem.191.4.587.

Tyrosine-phosphorylated bacterial proteins: Trojan horses for the host cell

A Covacci  1 , R Rappuoli
Affiliations
Review

Tyrosine-phosphorylated bacterial proteins: Trojan horses for the host cell

A Covacci et al. J Exp Med. .
No abstract available

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Figures

Figure 1
Figure 1
Schematic representation of a bacterial flagellum (a) and a conjugative pilus (b) showing their similarity to type III and type IV secretion systems, respectively. In a, the structural similarities between the core structures of the flagellar apparatus and the type III secretion system are sketched. In b, a hypothetical conjugative apparatus and a type IV system are reduced to an artistic impression; the proteic subunits forming the structure are not represented.
Figure 2
Figure 2
After type IV contact and CagA translocation, two independent signaling pathways are induced in the host cell.
Figure 3
Figure 3
Type III and type IV secretion systems functionally converge. Enteropathogenic E. coli and H. pylori (a) inject tyrosine-phosphorylated effector proteins by type III or type IV engines, respectively. (b) Tir is the EPEC receptor for intimin (binary products of the LEE [locus of enterocyte effacement] pathogenicity island). CagA is a Helicobacter-translocated molecule. (c) After phosphorylation on a tyrosine residue by a host cell kinase, cortical actin polymerization and pedestal protrusion are induced. Both microorganisms promote similar cellular responses.
See this image and copyright information in PMC

Comment on

References

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