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Review
. 2001 Mar;69(3):1231-43.
doi: 10.1128/IAI.69.3.1231-1243.2001.

Virulence functions of autotransporter proteins

I R Henderson  1 , J P Nataro
Affiliations
Review

Virulence functions of autotransporter proteins

I R Henderson et al. Infect Immun. 2001 Mar.
No abstract available

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Figures

FIG. 1
FIG. 1
Model of autotransporter (type V) secretion mechanism. Proteins exported by the autotransporter secretion mechanism are translated as a polyprotein possessing three domains. The three domains of the polyprotein (the leader sequence, the passenger domain, and the C-terminal β-domain) are indicated. The leader sequence directs secretion via the sec apparatus and is cleaved at the inner membrane by a signal peptidase releasing the remaining portion of the molecule into the periplasm. Once in the periplasm the β-domain assumes a biophysically favored state characterized by a β-barrel shaped structure which inserts itself into the outer membrane to form a pore. After insertion into the outer membrane the passenger domain is translocated to the bacterial cell surface where it may remain intact or undergo processing. A processed protein may be released into the extracellular milieu or remain associated with the bacterial cell surface.
FIG. 2
FIG. 2
Phylogenetic distribution of the autotransporters. (A) Phylogenetic tree of the eubacteria based on 16S rRNA sequences. The tree contains a detailed list of the gram-negative proteobacteria and their subdivisons (identified by Greek symbols) and was adapted from information appearing elsewhere (137) and at the Bergey's Manual Trust website (http://www.cme.msu.edu/Bergeys/btcomments/bt9.pdf). Genera for which autotransporters have been identified and characterized are indicated by boldface. The number of autotransporters identified per genus is given in parentheses after the genus name. (B) Phylogenetic tree of the autotransporter proteins inferred from comparison of the complete amino acid sequences of the polyproteins. The sequences were aligned using the multisequence alignment program CLUSTALX. Phylogenetic relationships and evolutionary distances were calculated, and a dendrogram was constructed using the neighbor-joining method. The positions of the autotransporter proteins within the tree are indicated by families such that the IgA1 proteases from Neisseria meningitidis and N. gonorrhoeae and H. influenzae cluster in the IgA1 protease family, etc.
FIG. 3
FIG. 3
Toxic effects of Pet. Both treated (A) and untreated (B) HEp-2 epithelial cells were incubated for 6 h at 37°C in culture medium without antibiotics and serum. Release of cellular focal contacts from the glass substratum, rounding of the cells, and cell detachment from the glass substratum are features consistently observed after treatment with Pet. Remnant cells after almost complete detachment of cells from the glass substratum are visible in panel A. Scanning electron photomicrographs of in vitro-cultured human colonic tissues infected with wild-type enteroaggregative E. coli expressing Pet (C) and an insertional mutant strain not expressing the protein (D) are also shown. The surface of the colon specimen shown in panel C is abnormal compared to that shown in panel D, as manifested by increased crypt aperture (arrowheads) and goblet cell pitting (arrows) when compared Bars, 50 μm.
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References

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