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Color Plates

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Figures

Image of Figure 1.3

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Figure 1.3

action tails. (Left top and bottom) Actin tails visualized by immunoflourescence. -infected cells were labeled with flourescein isothiocyanate-conjugated phalloidin (to label F-actin) and anti- antibodies. (Right) Actin tails visualized by electron microscopy. (Top) Thin-section electron micrograph from an infected tissue culture cell showing a moving bacterium associated with an F-actin comet tail (Tilney technique). (Middle) Three-dimensional visualization of the actin comet tail by the quick-freeze/deep-etch technique (courtesy of J. Heuser). (Bottom) Thin section through an cell with a tail whose actin filaments have been decorated with subfragment 1 (S1) of myosin.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 3.1

General cell organization (see text for details).

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 6.2

Immunofluorescence microscopic localization of the main forms of integrin-mediated matrix adhesions. Human foreskin fibroblast, labeled for phosphotyrosine, displaying mainly “classical” focal adhesions, located primarily at the cell periphery. Fibrillar adhesions of human foreskin fibroblast labeled for tensin. These adhesions are typically associated with fibronectin fibrils and are enriched in central regions of the cells. Human fibroblasts (SV80 line) treated with the Rho-kinase inhibitor Y-27632 and immunolabeled for phosphotyrosine. The labeling is associated primarily with small dot-like structures associated with the lamellipodium, which are identified morphologically as focal complexes. Paxillin-labeled podosomes formed by a primary rat osteoclast. Individual podosomes consist of a ring containing several “plaque proteins” (see insert), and an actin-rich central domain. As seen in this picture, podosomes often tend to cluster into large arrays. Reproduced with permission from (Geiger et al., 2001), Macmillan Magazines Ltd.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 6.4

(Top) Double fluorescent labeling of fibroblasts for actin (green) and vinculin or paxillin (red). (Bottom) Double immunofluorescence labeling (right) for vinculin (red) and α integrin (green) or (left) for paxillin (red) and phosphotyrosine (PY) (green). Both vinculin and paxillin are associated with the termini of actin-containing stress fibers. Vinculin and phosphotyrosine are also associated with cell-cell adherens junctions, while paxillin and integrin are present only in matrix adhesions.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 6.5

Components of cell-cell adherens junctions. (Top) Double immunofluorescence labeling of epithelial MDCK cells for cadherin (red) and β-catenin (green). Cell-cell junctions are seen as yellow lines due to superposition of red and green colors, showing nearly complete overlap between cadherin and β-catenin at cell-cell adhesion. (Bottom) Overexpression of a chimeric molecule consisting of β-catenin and green fluorescent protein (which allows visualization of the molecule) in MDCK cells by transient transfection followed by immunolabeling for cadherin (red). The fluorescent β-catenin appears green. Note that when overexpressed, β-catenin accumulates in the nucleus, forming aggregates of different shapes.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 6.6

A scheme summarizing known interactions between the various constituents of cell-matrix adhesions. Components that were found to be associated with cell-matrix adhesion sites are placed inside the internal green box, whereas additional selected proteins that affect matrix adhesions but were not reported to stably associate with them are placed in the external blue frame. The general property of each component is indicated by the color of its box, and the type of interaction between the components is indicated by the style and color of the interconnecting lines, as indicated in the legend. From Zamir and Geiger (2001).

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 10.8

Phase-contrast and fluorescence micrographs of a tachyzoite of caught in the act of invading a mammalian cell. The preparation was reached with antibody against the parasite surface protein SAG1 permeabilized, and incubated with antibody against the microneme protein MIC2 The fluorescence shows the capping of the surface protein SAG1 concomitant with the secretion of the microneme protein MIC2 into the nascent parasitophorous vacuole during the entry process. The junction point between the parasite and the host cell is indicated by an arrow. The parasite is known to remodel this vacuole extensively during establishment of intracellular infection. Courtesy of L. David Sibley.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 15.6

Structural analysis of type III secretion chaperones. Molecular architecture of the SicP chaperone from consists of two sets of tightly bound homodimers. Shown is the surface distribution of polar regions (grey) and hydrophobic regions (yellow). The SicP homodimer pairs are encased in a complex with two SptP effector molecules (simplistically shown as a red and blue ribbon) that lie within a helix-binding grove. The effector-interacting surfaces of SicP are predominantly hydrophobic. Modified from Figure 4 in C. E. Stebbins and J. E. Galán, 77–81, 2001, with permission and provided by Jorge Galán, Yale University School of Medicine, New Haven, Conn. A proposed model for the chaperone-mediated secretion of type III substrates. As a prerequisite for translocation into a target eukaryotic cell, an effector substrate binds to a cognate chaperone homodimer. At this site of binding (near the N-terminus), localized effector unfolding occurs, while the C-terminal enzymatic domain remains folded and functionally active (depicted by a gold globular shape). This effector – chaperone complex probably docks at the inner face of the type III secreton. Localized unfolding may ‘catalyze’ a general unfolding along the entire effector as it is secreted through the secreton. The chaperone homodimer is released and might be recycled to form a complex with another newly synthesized cognate effector molecule pre-destined for secretion.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 15.7

-induced translocation of Yops into cultured HeLa cells. Translocation of Yops is visualized by confocal laser-scanning microscopy. Yops are represented by green fluorescence: YopH (A), YopE (B), and YpkA (C). HeLa cell plasma membranes are illustrated by the red fluorescence. Note that the individual Yops have different locations within the eukaryotic cell: YopH is widely distributed in both the cytosolic and nuclear compartments, YopE is enriched in the perinuclear region, and YpkA is localized at the inner surface of the plasma membrane. Yellow indicates colocalization of YpkA and the plasma membrane. Mutants in any of or are translocation deficient.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 20.2

Gene expression experiment performed on a microarray. Flow of a microarray experiment. Scanned image of hybridized microarray and close-up image showing three possible outcomes of hybridization.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 20.6

GFP as a tool to detect gene expression in intracellular bacteria. Mouse macrophages were infected with serovar Typhimurium containing a reporter gene fused to a promoter expressed only when the bacteria reside within host cells. Bacteria inside cells appear as green rods while bacteria outside (stained with an anti- antibody conjugated to Texas Red) do not express GFP.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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Figure 23.5

Bacterial and fungal pathogens but not innocuous bacteria or yeast accumulate in the intestine. In most, but not all cases, killing of by microbial pathogens involves the accumulation of the pathogenic microbe in the intestine. Normally, when is feeding on a relatively innocuous bacterium such as expressing green fluorescent protein (GFP) as in this photomicrograph, almost all the ingested bacteria are ground up in the pharyngeal grinder organ and very few intact bacteria enter the intestinal lumen. Similarly, when feeding on the innocuous yeast no intact yeast cells can be observed in the intestine. In this latter case, the yeast cells are large enough to be readily seen without being labeled by GFP. In contrast to the results obtained with innocuous microbes, when feeding on most pathogenic bacteria or yeast, such as or pictured here, high titers of the pathogenic microbes accumulate in the intestine.

Citation: Cossart P, Boquet P, Normark S, Rappuoli R. 2004. Color Plates, In Cellular Microbiology, Second Edition. ASM Press, Washington, DC.
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