Biochemical and Functional Analyses of the Mip Protein: Influence of the N-Terminal Half and of Peptidylprolyl Isomerase Activity on the Virulence of
            <i>Legionella pneumophila</i>

Köhler, R.; Fanghänel, Jörg; König, Bettina; Lüneberg, Edeltraud; Frosch, Matthias; Rahfeld, Jens‐Ulrich; Hilgenfeld, Rolf; Fischer, Gunter; Hacker, Jörg; Steinert, Michael

doi:10.1128/iai.71.8.4389-4397.2003

Cited by 72 publications

(93 citation statements)

References 52 publications

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“…There is evidence that PPIases contribute to bacterial infection and virulence. The Mip protein of Legionella pneumophila, a member of the FK506-binding protein family, is involved in its entry into host cells and intracellular replication (47). The streptococcal cyclophilin SlrA is involved in pneumococcal colonization (48).…”

Section: Discussionmentioning

confidence: 99%

TLR4-Dependent NF-κB Activation and Mitogen- and Stress-Activated Protein Kinase 1-Triggered Phosphorylation Events Are Central to Helicobacter pylori Peptidyl Prolyl cis-, trans-Isomerase (HP0175)-Mediated Induction of IL-6 Release from Macrophages

Pathak

Basu

Bhattacharyya

et al. 2006

The Journal of Immunology

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Helicobacter pylori infection is associated with the local production of chemokines and cytokines, of which IL-6 is overexpressed at the margin of gastric ulcer in H. pylori-positive gastritis. Cells of the monocytic lineage are the major sources of IL-6, and mononuclear cell infiltration in the lamina propria is characteristic of H. pylori-induced chronic infection. Our study shows for the first time that a secreted peptidyl prolyl cis-, trans-isomerase, HP0175 elicits IL-6 gene expression and IL-6 release from macrophages. An isogenic strain inactivated in the HP0175 gene (knockout) was attenuated in its IL-6-inducing ability, which was restored after complementation with the HP0175 gene. The specificity of the HP0175-induced effect was confirmed by the fact that rHP0175 purified from HEK293 cells could also induce IL-6 release, ruling out the possibility that the observed effect was due to bacterial contaminants. HP0175 was capable of interacting directly with the extracellular domain of TLR4. HP0175-induced IL-6 gene expression was critically dependent on TLR4-dependent NF-κB and MAPK activation. TLR4/PI3K-dependent ERK1/2 and p38 MAPK signaling converged upon activation of mitogen- and stress-activated protein kinase 1 (MSK1). The central role of MSK1 was borne out by the fact that silencing of MSK1 expression abrogated HP0175-mediated NF-κB-dependent IL-6 gene transcription. MSK1 regulated the recruitment of p65 and phopho-Ser10-histone H3 to the IL-6 promoter. HP0175 therefore regulated IL-6 gene transcription through chromatin modification at the IL-6 promoter.

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Section: Discussionmentioning

confidence: 99%

TLR4-Dependent NF-κB Activation and Mitogen- and Stress-Activated Protein Kinase 1-Triggered Phosphorylation Events Are Central to Helicobacter pylori Peptidyl Prolyl cis-, trans-Isomerase (HP0175)-Mediated Induction of IL-6 Release from Macrophages

Pathak

Basu

Bhattacharyya

et al. 2006

The Journal of Immunology

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“…While the monomer retained its enzymatic activity in peptide folding assays, in protein folding experiments with denatured RCM-T 1 as substrate, a significant loss in activity was observed (Köhler et al, 2003). Interestingly, in cell culture and guinea pig infections complementing the mutant with monomeric Mip reverted the phenotype only to a limited degree.…”

Section: Mip Of Legionella Pneumophilamentioning

confidence: 97%

“…Moreover, the Tyr185Ala mutant with 1-2 % PPIase activity also failed to complement the phenotype back to wild type levels. Hence, infection studies suggest that for complete Mip action in vivo, the dimeric nature of the protein is substantial, and that the PPIase and the N-terminal accessory chaperone activity, which is not yet in detail described, need to act in a concerted fashion (Köhler et al, 2003).…”

Section: Mip Of Legionella Pneumophilamentioning

confidence: 99%

FKBPs in bacterial infections

Ünal

Steinert

2015

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…It has been shown that, for L. pneumophila to have its full virulence in higher organisms, such as guinea pigs, both the full-length Mip protein and PPIase activity are necessary [100]. While the Mip protein is important for invasion and establishment within human macrophages and protozoa, it is not necessary for intracellular replication.…”

Section: Legionella Pneumophila Life Cyclementioning

confidence: 99%

Knowledge to Predict Pathogens: Legionella pneumophila Lifecycle Critical Review Part I Uptake into Host Cells

Mraz

Weir

2018

Water

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Legionella pneumophila (L. pneumophila) is an infectious disease agent of increasing concern due to its ability to cause Legionnaires' Disease, a severe community pneumonia, and the difficulty in controlling it within water systems. L. pneumophila thrives within the biofilm of premise plumbing systems, utilizing protozoan hosts for protection from disinfectants and other environmental stressors. While there is a great deal of information regarding how L. pneumophila interacts with protozoa and human macrophages (host for human infection), the ability to use this data in a model to attempt to predict a concentration of L. pneumophila in a water system is not known. The lifecycle of L. pneumophila within host cells involves three processes: uptake, growth, and egression from the host cell. The complexity of these three processes would risk conflation of the concepts; therefore, this review details the available information regarding how L. pneumophila invades host cells (uptake) within the context of data needed to model this process, while a second review will focus on growth and egression. The overall intent of both reviews is to detail how the steps in L. pneumophila's lifecycle in drinking water systems affect human infectivity, as opposed to detailing just its growth and persistence in drinking water systems.

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Biochemical and Functional Analyses of the Mip Protein: Influence of the N-Terminal Half and of Peptidylprolyl Isomerase Activity on the Virulence of Legionella pneumophila

Cited by 72 publications

References 52 publications

TLR4-Dependent NF-κB Activation and Mitogen- and Stress-Activated Protein Kinase 1-Triggered Phosphorylation Events Are Central to Helicobacter pylori Peptidyl Prolyl cis-, trans-Isomerase (HP0175)-Mediated Induction of IL-6 Release from Macrophages

TLR4-Dependent NF-κB Activation and Mitogen- and Stress-Activated Protein Kinase 1-Triggered Phosphorylation Events Are Central to Helicobacter pylori Peptidyl Prolyl cis-, trans-Isomerase (HP0175)-Mediated Induction of IL-6 Release from Macrophages

FKBPs in bacterial infections

Knowledge to Predict Pathogens: Legionella pneumophila Lifecycle Critical Review Part I Uptake into Host Cells

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