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EcoSal Plus

Domain 8:

Pathogenesis

Autotransporter Proteins

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  • Authors: Ian R. Henderson1, and James P. Nataro2
  • Editor: Michael S. Donnenberg3
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Bacterial Pathogenesis and Genomics Unit, Division of Immunity and Infection, University of Birmingham, Birmingham B15 2TT, United Kingdom; 2: Center for Vaccine Development, Department of Pediatrics, University of Maryland School of Medicine, 685 W. Baltimore St., Baltimore, MD 21201; 3: University of Maryland, School of Medicine, Baltimore, MD
  • Received 03 February 2005 Accepted 16 May 2005 Published 01 November 2005
  • Address correspondence to James P. Nataro jnataro@medicine.umaryland.edu
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  • Abstract:

    This review focuses on the function of the and autotransporters for which a considerable amount of literature is available. Members of the serine protease autotransporters of the (SPATEs) family are proteins from and spp., which, like the and IgA1 proteases and Hap, possess a consensus serine protease motif. The largest subfamily of autotransporters is defined by the AidA conserved domain COG3468 and consists of members from a diverse range of animal and plant pathogens including , , . This subfamily, which is composed of more than 55 proteins, possesses some of the best-characterized autotransporter proteins including the mediator of motility IcsA, the major phase-variable outer membrane protein antigen 43 (Ag43) and the diffuse adhering (DAEC) adhesin AIDA-I, from which this subfamily derives its name. Another member of the AIDA-I family, and one of the most studied autotransporter proteins, is IcsA. The autotransporter pathway is emerging as the most common mechanism of protein translocation across the gram-negative outer membrane.

  • Citation: Henderson I, Nataro J. 2005. Autotransporter Proteins, EcoSal Plus 2005; doi:10.1128/ecosalplus.8.7.3

Key Concept Ranking

Type V Secretion Systems
0.4221839
Outer Membrane Proteins
0.35926095
Reverse Transcriptase PCR
0.33457285
Urinary Tract Infections
0.3266507
0.4221839

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/content/journal/ecosalplus/10.1128/ecosalplus.8.7.3
2005-11-01
2017-07-27

Abstract:

This review focuses on the function of the and autotransporters for which a considerable amount of literature is available. Members of the serine protease autotransporters of the (SPATEs) family are proteins from and spp., which, like the and IgA1 proteases and Hap, possess a consensus serine protease motif. The largest subfamily of autotransporters is defined by the AidA conserved domain COG3468 and consists of members from a diverse range of animal and plant pathogens including , , . This subfamily, which is composed of more than 55 proteins, possesses some of the best-characterized autotransporter proteins including the mediator of motility IcsA, the major phase-variable outer membrane protein antigen 43 (Ag43) and the diffuse adhering (DAEC) adhesin AIDA-I, from which this subfamily derives its name. Another member of the AIDA-I family, and one of the most studied autotransporter proteins, is IcsA. The autotransporter pathway is emerging as the most common mechanism of protein translocation across the gram-negative outer membrane.

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Figures

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Figure 1

The secretion pathway of the autotransporters proteins (type Va) is depicted on the bottom left of the diagram, the two-partner system (type Vb) is in the center of the diagram, and the Oca family (type Vc) is on the right of the figure. The four functional domains of the proteins are shown: the signal sequence, the passenger domain, the linker region, and the β-domain. The autotransporter polyproteins are synthesized and generally exported through the cytoplasmic membrane via the Sec machinery. Effector proteins with an unusual extended signal sequence, which purportedly mediates Srp-dependent export, are found in all three categories of type V secretion. Once through the inner membrane, the signal sequence is cleaved and the β-domain inserts into the outer membrane in a biophysically favored β-barrel structure that forms a pore in the outer membrane. After formation of the β-barrel, the passenger domain inserts into the pore and is translocated to the bacterial cell surface where it may or may not undergo further processing. Figure courtesy of Henderson et al. ( 1 ).

Citation: Henderson I, Nataro J. 2005. Autotransporter Proteins, EcoSal Plus 2005; doi:10.1128/ecosalplus.8.7.3
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Figure 2

Phylogenetic tree of the ECOR isolates showing the distribution of vat- and SPATE-encoding genes where each locus is represented by a shaded box as indicated in the figure. The number of the ECOR isolate is given in boldface, and each of the major phylogenetic branches is indicated. The complete complement of virulence-associated loci is preferentially associated with the B2 phylogenetic cluster. Figure adapted from Parham et al. ( 21 ).

Citation: Henderson I, Nataro J. 2005. Autotransporter Proteins, EcoSal Plus 2005; doi:10.1128/ecosalplus.8.7.3
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Figure 3

Trees were further tested for reliability using bootstrap analysis, yielding results of 96.9% (A) and 99.4% (B). In panel A the known substrates or effect for each SPATE is indicated.

Citation: Henderson I, Nataro J. 2005. Autotransporter Proteins, EcoSal Plus 2005; doi:10.1128/ecosalplus.8.7.3
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Figure 4

(A) Cleavage of protein substrates by SPATE proteins. I, Spectrin. One microgram of spectrin purified from sheep red blood cells was incubated with 1 μg of each SPATE protein overnight. The reaction products were separated on SDS–6% PAGE gels. II, Pepsin. Three micrograms of purified pepsin was incubated with 1 μg of each SPATE for 1 h at 37°C. The reaction products were separated on SDS–12% PAGE gels. III, Human coagulation factor V. A total of 2.5 μg of purified coagulation factor V was combined with 2 μg of each SPATE protein in a 40-μl total volume and incubated overnight. (B) Cleavage of bovine submaxillary mucus. Ten micrograms of each SPATE was incubated overnight at 37°C on medium containing 1.5% agarose and 1% bovine submaxillary mucus. Mucin was stained with 0.1% amido black. (C) Effects of SPATEs on HEp-2 cell monolayers are shown by oil immersion light microscopy of Giemsa-stained HEp-2 cells after treatment with SPATE proteins at 500 nM for 5 h. Rounding of cells is shown with Pet and Sat (arrows). Figure adapted from Dutta et al. ( 22 ).

Citation: Henderson I, Nataro J. 2005. Autotransporter Proteins, EcoSal Plus 2005; doi:10.1128/ecosalplus.8.7.3
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Figure 5

Internalization of Pet (A) and a serine protease motif mutant (Pet S260I) (B) into HEp-2 cells. HEp-2 cells were treated with either Pet or Pet S260I for 1 h. Actin cytoskeleton is labeled with green and Pet or Pet S260I is labeled with red. Note the perinuclear localization of Pet or Pet S260I inside the cells. Effect of Pet (C) or Pet S260I (D) on fodrin redistribution in HEp-2 cells. HEp-2 cells were treated with either Pet or Pet S260I for 3 h. Actin cytoskeleton is labeled with blue, Pet or Pet S260I with red, and fodrin with green. Note that Pet but not Pet S260I cause cytoskeletal damage and fodrin redistribution (arrows) and it is possible to detect a delayed interaction between Pet S260I and fodrin due to inability to cleave it (yellow dots). Scanning electron photomicrographs of in vitro-cultured human colonic tissues infected with the EAEC strain 042 (E) and the mutant strain JIF1 (F). For the tissue shown in panel E the surface of the colon is markedly abnormal, as manifested by increased crypt apertures (white arrowhead), prominent mucosal crevices (white arrow), goblet cell pitting (black arrowhead in a circle), and rounding of epithelial cells (black arrow in a circle). Figure courtesy of Henderson et al. ( 1 ).

Citation: Henderson I, Nataro J. 2005. Autotransporter Proteins, EcoSal Plus 2005; doi:10.1128/ecosalplus.8.7.3
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Tables

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Table 1

Functional classification and distribution of the and autotransporters

Citation: Henderson I, Nataro J. 2005. Autotransporter Proteins, EcoSal Plus 2005; doi:10.1128/ecosalplus.8.7.3

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