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Review
. 2007 Feb;75(2):545-52.
doi: 10.1128/IAI.01506-06. Epub 2006 Nov 21.

How flagellin and toll-like receptor 5 contribute to enteric infection

Theodore S Steiner  1
Affiliations
Review

How flagellin and toll-like receptor 5 contribute to enteric infection

Theodore S Steiner. Infect Immun. 2007 Feb.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Tertiary structure of flagellin and synthesis of flagella. (A) Schematic diagram of flagellin export and flagellum formation. Flagellin monomers (FliC) are synthesized and transported with a chaperone (FliS) to the inner membrane, where they are exported through the central pore of the flagellar basal body that straddles the inner membrane (IM) and outer membrane (OM) of the cell wall. FliC monomers continue through the pore of the flagellar filament, where they are added to the growing end beneath the cap protein (FliD). (B) Crystal structure of the F41 fragment of Salmonella FliC. The domains are labeled, and amino acids critical for TLR5 activation are indicated. (C) Space-filling model of flagellin, with sites of polymerization shown in the hypothetical flagellin trimer.
FIG. 2.
FIG. 2.
Primary sequences of the critical regions of conserved domains of flagellins from selected γ- and α- proteobacteria, numbered according to the E. coli H18 flagellin numbering system. The following regions are enclosed in boxes: the site of compensatory mutations that allow motility of α-proteobacteria (region A); two regions where substitutions eliminate TLR5 activity (regions B and D); and the site of a point mutation that most strongly eliminates TLR5 activity (region C). Information for individual residues is indicated as follows: asterisk, point mutation that reduces or eliminates activity; dagger, site of random transposon insertion that reduces or eliminates activity; 0, point mutation that preserves activity; double dagger, point mutation that reduces inflammatory activity yet preserves motility.
FIG. 3.
FIG. 3.
Schematic diagram of the various roles of flagellin in Salmonella gastroenteritis. A, internalization of organisms by epithelial cells, with membrane ruffling (SPI-1 dependent); B, transport of flagellin monomers through the epithelium to encounter basolateral TLR5 (SPI-1 dependent); C, encounter with lamina propria DC (flagellin activation of TLR5 may facilitate uptake and/or survival of organisms, which is also SPI-2 dependent); D, encounter with lamina propria macrophage (Mφ) (organisms are internalized). In resistant hosts, flagellin-dependent Ipaf recognition activates caspase-1, leading to IL-1 secretion and cell death. TLR5 is expressed on human macrophages but not on murine macrophages; the role of TLR5 in human salmonella gastroenteritis remains uncertain. LN, lymph nodes.
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References

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