Actin-Based Motility of Intracellular Microbial Pathogens

Goldberg, Marcia B.

doi:10.1128/mmbr.65.4.595-626.2001

Cited by 199 publications

(195 citation statements)

References 208 publications

(372 reference statements)

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“…7), and these strains were also able to form plaques and F-actin comet tails. The cell surface localization of IcsA in these strains and their phenotype is inconsistent with the hypothesis that strict polar IcsA localization is needed for ABM within cells (Goldberg, 2001;Suzuki & Sasakawa, 2001).…”

Section: Discussioncontrasting

confidence: 45%

“…al., 1997). IcsA is an outer-membrane protein that is essential for initiating ABM (Bernardini et al, 1989;Lett et al, 1989;Goldberg, 2001;Suzuki & Sasakawa, 2001). S. flexneri 2a additionally produces LPS with very long (VL) type Oag chains with a modal length of greater than 90 RUs; these are determined by the Wzz pHS2 (Cld pHS-2 ) protein, which is encoded by a small plasmid called pHS-2 (Stevenson et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

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Genetic modulation of Shigella flexneri 2a lipopolysaccharide O antigen modal chain length reveals that it has been optimized for virulence

2003

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The lipopolysaccharide (LPS) molecules of Shigella flexneri 2a have O antigen (Oag) polysaccharides with two modal chain length distributions. The chromosomal wzz SF gene results in short (S) type Oag chains [11-17 Oag repeat units (RUs)], and the pHS-2 plasmid-located wzz pHS2 gene results in very long (VL) type Oag chains (>90 Oag RUs). S. flexneri wzz SF mutants are unable to form plaques on HeLa cell monolayers and F-actin comet tails, indicating that IcsA/ VirG function in actin-based motility (ABM) is defective. An S. flexneri wzz SF wzz pHS2 double mutant had LPS with relatively short, random length Oag chains and, paradoxically, was able to form plaques and F-actin comet tails. The influence of Oag modal chain length distribution on virulence and related properties was investigated using complementation with different wzz genes. Wzz O139 from Vibrio cholerae O139 and Wzz ST from Salmonella enterica serovar Typhimurium were fully functional in Shigella flexneri, resulting in LPS with either very short (VS) type Oag chains (2-7 Oag RUs) or long (L) type Oag chains (19-35 RUs), respectively. In the absence of VL-type Oag chains, the VS-, S-and L-type Oag chains were permissive for plaque and F-actin comet tail formation. However, in the presence of LPS with VL-type Oag chains, the VS-and S-type Oag chains but not the L-type Oag chains were permissive for plaque and F-actin comet tail formation. These data, and the results of a previous investigation, show that IcsA function in ABM requires LPS Oag chains with at least two but less than 18 RUs when VL-type Oag chains are co-expressed on the cell surface. However, in the absence of the VL-type Oag chains, LPS Oag chains with at least two but less than 90 RUs are able to support IcsA function in ABM. Indirect immunofluorescence staining of IcsA on the cell surface of the S. flexneri strains did not correlate with the observed effect of Oag chain length on plaque and F-actin comet tail formation. However, when intracellular bacteria lacking VL-type Oag chains were examined, an inverse correlation between Oag modal chain length and detection of IcsA was observed, i.e. staining decreased with increased modal length. It is hypothesized that Oag chains can mask IcsA and interfere with its function in ABM, and a model is presented to explain how LPS Oag and IcsA may interact. It is suggested that S. flexneri 2a has evolved to synthesize LPS with two Oag modal chain lengths, as S-type Oag chains allow IcsA to function in ABM in the presence of VL-type Oag chains that confer resistance to serum.

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Section: Discussioncontrasting

confidence: 45%

Section: Introductionmentioning

confidence: 99%

Genetic modulation of Shigella flexneri 2a lipopolysaccharide O antigen modal chain length reveals that it has been optimized for virulence

2003

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“…The average lateral displacement quantified for sixteen moving spots identified from three cells was 2.16±0.25 µm, and the average lateral speed of these motile spots was 0.84±0.10 µm second -1 . This is greater than the speed of actin-based motility for listeria (Goldberg, 2001) or vesicle-based movement (Merrifield et al, 1999) and is consistent with some of the rates of movement of microtubules motors (Apodaca, 2001) and myosin-V-based transport (Tabb et al, 1998).…”

Section: Resultsmentioning

confidence: 82%

Real-time analysis of clathrin-mediated endocytosis during cell migration

Rappoport

Simon

2003

Journal of Cell Science

165

161

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. Real-time analysis of clathrin-mediated endocytosis during cell migration. J. Cell Sci. 116, 847-855.In both the online and print versions of this paper, in Materials and Methods, the construct pEGFP-dynamin2 was incorrectly identified as a human isoform. It is a rat isoform. AUTHOR CORRECTION IntroductionThe internalization of integral membrane proteins from the cell surface through receptor-mediated endocytosis occurs via clathrin-coated pits (Schmid, 1997;Takei and Haucke, 2001). Examples of molecules that undergo clathrin-mediated endocytosis include nutrients such as iron, via transferrin uptake (Hopkins et al., 1985;Conrad et al., 1999), growth factors and cytokines, through receptors such as the epidermalgrowth-factor receptor (Lamaze and Schmid, 1995;Carter and Sorkin, 1998), and cellular adhesion molecules such as integrins (Raub and Kuentzel, 1989). Additionally, numerous pathogenic organisms and molecules have been observed to gain entry into cells by exploiting the endocytosis machinery (Doxsey et al., 1987;Sieczkarski and Whittaker, 2002). Endocytosis has also been implicated in cell migration (Bretscher, 1996;Palecek et al., 1996;Sheetz et al., 1999;Bajno et al., 2000;Kamiguchi and Lemmon, 2000). In particular, it has been proposed that an increased rate of endocytosis at the trailing edge would contribute to the polarized cycling of either bulk membrane or cellular adhesion molecules, such as integrins, to the leading edge (Bretscher, 1996;Palecek et al., 1996;Sheetz et al., 1999).Great strides have recently been made in the analysis of the different factors involved in the production of clathrin-coated vesicles (Takei and Haucke, 2001). The presence and interaction of such components as the AP-2 adapter complex (Benmerah et al., 1998;Kamiguchi et al., 1998) and the accessory proteins AP180 (Takei and Haucke, 2001), Eps15 (Benmerah et al., 1998;Benmerah et al., 1999) and Hip1R (Engqvist-Goldstein et al., 2001) are beginning to be well characterized. Many of the proteins that are involved in clathrin-mediated endocytosis have been identified and cloned, their crystal structures have been determined (ter Haar et al., 1998;Collins et al., 2002), and detailed models for the production and internalization of clathrin-coated vesicles have been suggested (Schmid, 1997;Takei and Haucke, 2001;Kirchhausen, 2002). However, numerous questions regarding the events and interactions relevant to endocytosis remain unanswered. For example, it is not clear whether activated receptors recruit AP-2 which results in the polymerization of clathrin coat components, or if clathrin-coated pits are preformed and recruit activated receptors. Additionally, the precise molecular function(s) of the GTPase dynamin in endocytosis remains to be resolved (Takei et al., 1995;Cao et al., 1998;McNiven et al., 2000;Ochoa et al., 2000;Schmid and Sorkin, 2002;Tsuboi et al., 2002). Although previous studies have focused on the neuron-specific dynamin1 isoform (Tsuboi et al., 2002), there is also a functional role in endocytosis for the...

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“…In host cells, the Arp2/3 complex is activated by nucleation-promoting factors including members of the Wiskott-Aldrich syndrome protein (WASP) family of proteins (Higgs & Pollard, 2001;Welch & Mullins, 2002). The mechanisms of activation of the Arp2/3 complex by intracellular pathogens are that they express surface proteins that recruit host WASP family proteins (e.g., S. flexneri IcsA), or they express functional mimics of WASPs (e.g., L. monocytogenes ActA) (Goldberg, 2001). It was proposed that actin in Rickettsia comet tails is nucleated by the host Arp2/3 complex, and the bacterial protein RickA has been shown to assemble branched actin networks in vitro (Jeng et al, 2004;Gouin et al, 2004) .…”

Section: Actin-based Mobility: Like Other Intracytosolic Bacteria Sucmentioning

confidence: 99%