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Yersinia infection tools-characterization of structure and function of adhesins - PubMed

  • ️Tue Jan 01 2013

Review

Yersinia infection tools-characterization of structure and function of adhesins

Kornelia M Mikula et al. Front Cell Infect Microbiol. 2013.

Abstract

Among the seventeen species of the Gram-negative genus Yersinia, three have been shown to be virulent and pathogenic to humans and animals-Y. enterocolitica, Y. pseudotuberculosis, and Y. pestis. In order to be so, they are armoured with various factors that help them adhere to tissues and organelles, cross the cellular barrier and escape the immune system during host invasion. The group of proteins that mediate pathogen-host interactions constitute adhesins. Invasin, Ail, YadA, YadB, YadC, Pla, and pH 6 antigen belong to the most prominent and best-known Yersinia adhesins. They act at different times and stages of infection complementing each other by their ability to bind a variety of host molecules such as collagen, fibronectin, laminin, β1 integrins, and complement regulators. All the proteins are anchored in the bacterial outer membrane (OM), often forming rod-like or fimbrial-like structures that protrude to the extracellular milieu. Structural studies have shown that the anchor region forms a β-barrel composed of 8, 10, or 12 antiparallel β-strands. Depending on the protein, the extracellular part can be composed of several domains belonging to the immunoglobulin fold superfamily, or form a coiled-coil structure with globular head domain at the end, or just constitute several loops connecting individual β-strands in the β-barrel. Those extracellular regions define the activity of each adhesin. This review focuses on the structure and function of these important molecules, and their role in pathogenesis.

Keywords: X-ray structure; Yersinia enterocolitica; Yersinia pestis; Yersinia pseudotuberculosis; adhesins; bacterial; outer membrane proteins; structure–function relationship.

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Figures

Figure 1
Figure 1

Schematic overview of proteins expressed in Yersiniae outer membrane during infection. Bacterial outer membrane (OM) with outer core of LPS (OC) in purple and adhesins expressed at different stages of infection. (A) Adhesisn of Y. enterocolitica and Y. pseudotuberculosis: invasin in yellow, YadA in dark green, Ail in red, and O-Antigen in light grey; (B) Adhesins of Y. pestis: Pla in green, YadB in blue, YadC in orange, Ail in red. ECM stands for extracellular matrix. All the molecules are on approximately the same scale.

Figure 2
Figure 2

Modular architecture of the Y. pseudotuberculosis invasin. (A) A schematic topology model of preprotein. From N-terminus: (SP) signal peptide, (a) periplasmic hydrophilic α-domain, (β-barrel) OM embedded β-barrel domain, (α') periplasmic hydrophilic α'-domain, (D1–D4) extracellular Ig-like domains, (D5) extracellular distal domain of the C-type lectin-like fold. D4 and D5 form a functional integrin binding module. (B) Ribbon diagram of the structure of D1–D5 (1CWV). Residues D811, R883, C907, D911, and C982 (space-filling representation) are implicated in integrin binding. (C) Ribbon diagram of the β-barrel structure (4E1T).

Figure 3
Figure 3

The ribbon diagrams of YadA. (A) A general topology model of YadA created based on the experimental structure of the head region and modeled stalk and anchor regions (Koretke et al., 2006). Modular organization and binding regions for different ligands are annotated. (B) The crystal structure of the YadA head domain from Y. enterocolitica (1P9H). Left panel is a side view showing the LPBR fold. The top view on the right panel presents trimeric organization of YadA.

Figure 4
Figure 4

The crystal structure of Ail from Y. pestis. Topology diagram of the Ail structure (3QRA) with partially disordered loops two (L2) and three (L3). The invisible loop regions are marked on the picture as violet dashed lines. Residues D93 and F94 (crucial in serum resistance and invasion) are shown as sticks.

Figure 5
Figure 5

The crystal structure of Pla from Y. pestis. Topology diagrams of the Pla structure (2X55). (A) Side view presenting the position of the putative LPS binding site (residues D84, D86, D206, and H208 in stick representation). (B) Top view showing the active site. D84 and D86 coordinate nucleophilic water molecule W1 either directly or indirectly via second water molecule W2. D206 and H208, the latter being hydrogen bonded to W1, form a catalytic dyad.

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