Internalization and intracellular survival of Mycoplasma pneumoniae by non-phagocytic cells

Yavlovich, Amichai

doi:10.1016/j.femsle.2004.02.016

Cited by 46 publications

(56 citation statements)

References 21 publications

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“…Furthermore, Mycoplasma pneumoniae (Mp), which is the closest relative to Mg, achieves cytoplasmic and perinuclear localization in WI-38 (Baseman et al, 1995) by 2 h, and a similar localization was reported for this pathogen within the human hepatocyte cell line Hep-G2 (Meseguer et al, 2003). Yavlovich et al (2004) observed Mp internalization in human lung carcinoma A549 cells but not in HeLa epithelial cells. Finally, evidence for a nuclear locale for some mycoplasma species has been suggested.…”

Section: Discussionsupporting

confidence: 61%

Interaction of Mycoplasma genitalium with host cells: evidence for nuclear localization

et al. 2008

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Mycoplasma genitalium (Mg) is a mollicute that causes a range of human urogenital infections. A hallmark of these bacteria is their ability to establish chronic infections that can persist despite completion of appropriate antibiotic therapies and intact and functional immune systems. Intimate adherence and surface colonization of mycoplasmas to host cells are important pathogenic features. However, their facultative intracellular nature is poorly understood, partly due to difficulties in developing and standardizing cellular interaction model systems. Here, we characterize growth and invasion properties of two Mg strains (G37 and 1019V). Mg G37 is a high-passage laboratory strain, while Mg 1019V is a low-passage isolate recovered from the cervix. The two strains diverge partially in gene sequences for adherence-related proteins and exhibit subtle variations in their axenic growth. However, with both strains and consistent with our previous studies, a subset of adherent Mg organisms invade host cells and exhibit perinuclear targeting. Remarkably, intranuclear localization of Mg proteins is observed, which occurred as early as 30 min after infection. Mg strains deficient in adherence were markedly reduced in their ability to invade and associate with perinuclear and nuclear sites.

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Section: Discussionsupporting

confidence: 61%

Interaction of Mycoplasma genitalium with host cells: evidence for nuclear localization

et al. 2008

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“…Thus, in association with toxin-mediated epithelial cell damage, M. pneumoniae could also directly access subepithelial tissue targets and ECM by multiple pathways, including EF-Tu interactions with Fn. Further, these distinct pathogenic pathways may also contribute to the ability of M. pneumoniae to invade and establish intracellular and perinuclear residence (15,56). Taken together, these findings indicate that M. pneumoniae is a sophisticated and versatile bacterial pathogen with wide-ranging colonization strategies to overcome host defenses and trigger acute and chronic airway and extrapulmonary diseases.…”

Section: Discussionmentioning

confidence: 93%

The Surface-Exposed Carboxyl Region of Mycoplasma pneumoniae Elongation Factor Tu Interacts with Fibronectin

2008

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Mycoplasma pneumoniae is a bacterial pathogen of the human respiratory tract that causes a wide range of airway diseases as well as extrapulmonary symptoms. It possesses a distinct, differentiated terminal structure, termed the attachment organelle, that mediates adherence to the host respiratory epithelium. Previously, we reported that surface-associated M. pneumoniae elongation factor Tu (EF-Tu, also called MPN665) serves as a fibronectin (Fn)-binding protein, facilitating interactions between mycoplasmas and extracellular matrix. In the present study, we determined that binding of M. pneumoniae EF-Tu to Fn is primarily mediated by the EF-Tu carboxyl region. A 179-amino-acid region spanning the carboxyl terminus (designated EC; amino acids 192 to 394) binds Fn in a dose-dependent manner. Further analysis of carboxyl constructs (ED3 and ED4) and their deletion truncations (ED3.1, ED3.2, and ED4.1) revealed that the carboxyl region possessed two distinct sites with different Fn-binding efficiencies. Immunogold electron microscopy using antibodies raised against recombinant ED3 and ED4 demonstrated the surface accessibility of the EF-Tu carboxyl region. Competitive binding assays using intact radiolabeled mycoplasmas and purified recombinant ED3 and ED4 proteins, along with antibody blocking assays, reinforced the role of the surface-exposed EF-Tu carboxyl region in Fn binding. Alkali and high-salt treatment of mycoplasma membranes and Triton X-114-partitioned mycoplasma fractions confirmed the stable association of EF-Tu within the mycoplasma membrane. These observations highlight the unique, multifaceted, and unpredictable role of the classically defined cytoplasmic protein EF-Tu relative to cellular function, compartmentalization, and topography.

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“…Despite the apparent limitations suggested by its small genome, M. pneumoniae is a highly specialized pathogen that frequently causes upper and lower respiratory tract infections in humans, often resulting in atypical pneumonia [3]. Persistent infection is well documented in humans and animal models, and newer data confirm its ability to exist as a facultative intracellular pathogen [4][5][6], an observation which fits well with its small genome, the result of reductive genetic evolution and the signature of an intracellular organism [5].…”

Section: Introductionmentioning

confidence: 74%

Inhibition of message for FcεRI α chain blocks mast cell IL-4 production induced by co-culture with Mycoplasma pneumoniae

Luo

Dai

Duffy

et al. 2008

Microbial Pathogenesis

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We have previously described the activation of RBL-2H3 mast cells for IL-4 production by Mycoplasma pneumoniae but the mechanism remains unclear. M. pneumoniae binds eukaryotic cells primarily through sialoglycoproteins on the target cell surface. This study was undertaken to determine whether the sialated FcεRIα chain on RBL cells is important for M. pneumoniae-induced IL-4 production. We found that IgE-mediated IL-4 release by a series of RBL sublines correlated with the release induced by M. pneumoniae. Further, aggregation of FcγRII (CD32) in RBL cells using a monoclonal antibody inhibited both IgE-mediated and mycoplasma-induced IL-4 production, providing further evidence for an Fc receptor-mediated mechanism of activation. To examine the role of FcεRI in mycoplasma-induced IL-4 release, we created stably transfected RBL sublines using a vector expressing a short hairpin sequence designed to inhibit message for the FcεRI α chain. IgEinduced IL-4 production by the transfected sublines was reduced in similar proportion to the degree of message suppression. M. pneumoniae-induced IL-4 production in the four transfected sublines was completely blocked in contrast to results with the controls or parent RBL cells. We conclude that the heavily glycosylated FcεRI α chain is required for activation of mast cells for IL-4 production by M. pneumoniae.

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Internalization and intracellular survival of Mycoplasma pneumoniae by non-phagocytic cells

Cited by 46 publications

References 21 publications

Interaction of Mycoplasma genitalium with host cells: evidence for nuclear localization

Interaction of Mycoplasma genitalium with host cells: evidence for nuclear localization

The Surface-Exposed Carboxyl Region of Mycoplasma pneumoniae Elongation Factor Tu Interacts with Fibronectin

Inhibition of message for FcεRI α chain blocks mast cell IL-4 production induced by co-culture with Mycoplasma pneumoniae

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