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7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts

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7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts, Page 1 of 2

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Abstract:

This chapter focuses on a few examples of the involvement of cell adhesion molecules during infection, in interactions involved in processes such as adhesion or invasion, or in controlling the process of host inflammation. Adhesion molecules are cell surface receptors that establish cell-to-cell interactions, or interactions between cells and the extracellular matrix. The immunoglobulin superfamily of adhesion molecules is mostly involved in cell-to-cell interactions and consists of receptors with extracellular domains sharing homology with immunoglobulins. It is possible that interactions of proteoglycans with bacterial ligands participate in the initial stages of adhesion and that other types of interactions are involved either in stabilization of the bacterial adhesion processes or in invasion. Also, other Opa proteins bind to CD66 carcinoembryonic antigens, which are members of the Ig superfamily, and this interaction mediates bacterial internalization into host cells. For both and , the entry process appears to be driven by incremental interactions between bacterial surface ligands and cell adhesion molecules. Lipid rafts have changed our view of the classical membrane fluid mosaic model into a more complex system. Raft microdomains are described as dispersed liquid-ordered phase microdomains that diffuse laterally within the two-dimensional liquid-disordered phase membrane. The fact that cell surface receptors are dispensable for this type of bacterial signaling is not totally true because interactions between components of the and the αβ-integrin or the CD44 hyaluronic acid receptor were reported.

Citation: Tran Van Nhieu G, Sansonetti P, Lafont F. 2004. 7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts, p 139-156. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch7

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Figures

Image of Figure 7.1
Figure 7.1

Cell adhesion molecules: determinants of cell adhesion and cell–cell interactions. β integrins bind the extracellular matrix (ECM) via their extracellular domain and associate with the actin cytoskeleton via the cytoplasmic tail of the β subunit. Focal complexes are small β-integrin-containing adhesive structures that are formed upon activation of the small GTPase Rac. Focal adhesions, which are larger structures requiring Rho-dependent actomyosin contraction and connect to actin stress fibers, involve integrin clustering, tyrosylphosphorylation, and the recruitment of Src substrates. Cadherins establish homotypic interactions at cell-cell junctions and also associate with the cytoskeleton via their cytoplasmic tail. The formation of cadherin-based junctions depends on Rho GTPases. Members of the immunoglobulin (Ig) superfamily bind to a counter receptor, such as the LFA-1 (αβ) integrin or VCAM-1, on the surface of neutrophils and monocytes. Selectins bind to carbohydrate residues on the surface of leukocytes.

Citation: Tran Van Nhieu G, Sansonetti P, Lafont F. 2004. 7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts, p 139-156. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch7
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Image of Figure 7.2
Figure 7.2

Interactions of invading pathogens with an intestinal epithelium. The open arrows show potential interactions between the pathogen and cell adhesion molecules on the surface of various cell types during the invasion process. Bacteria that adhere to the apical surface of the epithelium often do so by establishing interactions with carbohydrate moieties or by a “bridging” mechanism (a). Invasive pathogens may enter via specialized cells, such as M cells present in the intestinal epithelium (b), and have elicited various ways to survive professional phagocytes (c). This encounter may result in the release of IL-1β and IL-18; and, in combination with IL-8 released by enterocytes, these cytokines contribute to recruit PMNs at the site of infection (d). Invasive pathogens that bind to cell receptors that are basolaterally distributed (open box) may then enter cells via the basolateral side, or via the apical side after receptor redistribution during a trauma or PMN transmigration (e).

Citation: Tran Van Nhieu G, Sansonetti P, Lafont F. 2004. 7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts, p 139-156. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch7
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Image of Figure 7.3
Figure 7.3

Modes of bacterial induced phagocytosis. invasin or internalin-mediated internalization results in bacteria surrounded by a tight phagosome. (Left) , high-affinity binding of invasin to integrins and integrin clustering are critical to drive the phagocytic process. The invasin-mediated bacterial internalization involves tyrosine kinase signaling, activation of the small GTPase Rac, and actin polymerization. (Right) Internalin mediates the internalization of by binding to E-cadherin. Bacterial uptake requires interaction between the cadherin cytoplasmic domain and catenins (cat). (Left) Type III secretory apparatus allows the targeting of bacterial effectors in the cell cytosol by means of a protein complex, the “translocon,” that inserts in the host cell membranes. A combination of bacterial type III effectors promotes bacterial internalization by regulating cytoskeletal reorganization at various levels. The IpaC protein, a component of the translocon (T), activates Src kinase signaling and actin polymerization dependent on the Cdc42 and Rac GTPases. The SopE and SptP proteins are a GEF and a GAP, respectively, for the GTPases Cdc42 and Rac. Cytoskeletal effectors correspond to bacterial type III effectors that associate with and regulate the function of cytoskeletal proteins, the SipA protein that binds to and stabilizes F-actin, and the IpaA protein that binds to the focal adhesion protein vinculin and induces actin depolymerization. Lipid phosphatase corresponds to the SopB or the IpgD protein that hydrolyzes PIP. (Right) The InlB protein binds to and activates the Met receptor. InlB binding to Met leads to tyrosine kinase signaling, recruitment of adapter proteins and of the PI-3 kinase, activation of the Rac GTPase, and actin cytoskeleton reorganization that drives the phagocytic process.

Citation: Tran Van Nhieu G, Sansonetti P, Lafont F. 2004. 7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts, p 139-156. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch7
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Figure 7.4

Two examples of up-regulation of adhesion molecules by bacterial pathogens. Up-regulation of the CR3 molecule as a means to enhance attachment of to leukocytes. Initial interaction of the bacterium (closed circle) with the cell leads to up-regulation of CR3 (filled box) and strengthens bacterial adhesion via FHA–CR3 interactions. Up-regulation of ICAM-1 (filled box) during infection leads to the recruitment of T cells and may indirectly participate in granuloma formation.

Citation: Tran Van Nhieu G, Sansonetti P, Lafont F. 2004. 7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts, p 139-156. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch7
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Tables

Generic image for table
Table 7.1

Cell adhesion molecules as receptors for bacterial pathogens

Citation: Tran Van Nhieu G, Sansonetti P, Lafont F. 2004. 7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts, p 139-156. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch7
Generic image for table
Table 7.2

Lipid rafts and bacterial pathogens

Citation: Tran Van Nhieu G, Sansonetti P, Lafont F. 2004. 7 Bacterial Signaling to Host Cells through Adhesion Molecules and Lipid Rafts, p 139-156. In Cossart P, Boquet P, Normark S, Rappuoli R (ed), Cellular Microbiology, Second Edition. ASM Press, Washington, DC. doi: 10.1128/9781555817633.ch7

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