Protein P200 Is Dispensable for
            <i>Mycoplasma pneumoniae</i>
            Hemadsorption but Not Gliding Motility or Colonization of Differentiated Bronchial Epithelium

Jordan, Jarrat L.; Chang, How-Yi; Balish, Mitchell F.; Holt, Lynley S.; Bose, Stephanie R.; Hasselbring, Benjamin M.; Waldo, Robert H.; Krunkosky, Thomas M.; Krause, Duncan C.

doi:10.1128/iai.01344-06

Cited by 51 publications

(59 citation statements)

References 37 publications

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“…The human pathogen M. pneumoniae has been shown to bind initially to the apical surface of ciliated human bronchial epithelial cells in vitro, then to move down towards the base of ciliated cells before spreading [38]. M. pneumoniae mutants that are defective in motility, but not in cytadherence, have impaired capacity to colonize differentiated bronchial epithelium in vitro [39], and these mutants cannot be recovered from the lung tissue four days after inoculation, whereas motile strains can be [40]. Gliding motility, therefore, seems to be * * * * Figure 6 Quantitative analysis of gliding motility.…”

Section: Discussionmentioning

confidence: 99%

First identification of proteins involved in motility of Mycoplasma gallisepticum

Indikova

Vronka

Szostak

2014

Vet Res

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Mycoplasma gallisepticum, the most pathogenic mycoplasma in poultry, is able to glide over solid surfaces. Although this gliding motility was first observed in 1968, no specific protein has yet been shown to be involved in gliding. We examined M. gallisepticum strains and clonal variants for motility and found that the cytadherence proteins GapA and CrmA were required for gliding. Loss of GapA or CrmA resulted in the loss of motility and hemadsorption and led to drastic changes in the characteristic flask-shape of the cells. To identify further genes involved in motility, a transposon mutant library of M. gallisepticum was generated and screened for motility-deficient mutants, using a screening assay based on colony morphology. Motility-deficient mutants had transposon insertions in gapA and the neighbouring downstream gene crmA. In addition, insertions were seen in gene mgc2, immediately upstream of gapA, in two motility-deficient mutants. In contrast to the GapA/CrmA mutants, the mgc2 motility mutants still possessed the ability to hemadsorb. Complementation of these mutants with a mgc2-hexahistidine fusion gene restored the motile phenotype. This is the first report assigning specific M. gallisepticum proteins to involvement in gliding motility.

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Section: Discussionmentioning

confidence: 99%

First identification of proteins involved in motility of Mycoplasma gallisepticum

Indikova

Vronka

Szostak

2014

Vet Res

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“…The attachment organelle is the leading end of the cell during gliding motility (Balish & Krause, 2006) and the location of the gliding motor ). Gliding appears to be important for spreading from the initial infection site (Jordan et al, 2007). Duplication of the M. pneumoniae attachment organelle at a site adjacent to the existing one accompanies initiation of DNA replication (Seto et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Attachment organelle ultrastructure correlates with phylogeny, not gliding motility properties, in Mycoplasma pneumoniae relatives

Hatchel

Balish

2008

Microbiology

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The Mycoplasma pneumoniae cluster is a clade of eight described species which all exhibit cellular polarity. Their polar attachment organelle is a hub of cellular activities including cytadherence and gliding motility, and its duplication in the species M. pneumoniae is coordinated with cell division and DNA replication. The attachment organelle houses a detergent-insoluble, electron-dense core whose presence is required for structural integrity. Although mutant analysis has led to the identification of attachment organelle proteins, the mechanistic basis for the activities of the attachment organelle remains poorly understood, with gliding motility attributed alternatively to the core or to the adhesins. In this study we investigated attachment organelle-associated phenotypes, including gliding motility characteristics and ultrastructural details, in seven species of the M. pneumoniae cluster under identical conditions, allowing direct comparison. We identified gliding ability in three species in which it has not previously been reported, Mycoplasma imitans, Mycoplasma pirum and Mycoplasma testudinis. Across species, ultrastructural features of attachment organelles and their cores do not correlate with gliding speed, and morphological features of cores are inconsistent with predictions about how these structures are involved in the gliding process, disfavouring a prominent, direct role for the electron-dense core in gliding. In addition, we found M. pneumoniae to be an outlier in terms of cell structure with respect to its close relatives, suggesting that it has acquired a special set of adaptations during its evolution.

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“…While the cytoskeletal protein HMW1 (MPN447) and membrane proteins P1, B/C, and P30 (MPN141, MPN142, and MPN453, respectively) localize to the terminal organelle and are required for gliding (5,(8)(9)(10), these proteins are also essential for cytadherence and attachment to surfaces. Accordingly, their distinct functions in gliding motility are difficult to define by mutagenesis alone.…”

mentioning

confidence: 99%

“…The gliding apparatus of M. pneumoniae is a polar terminal structure (6) that also functions in cell division (7) and adhesion to host receptors (2,5). While the cytoskeletal protein HMW1 (MPN447) and membrane proteins P1, B/C, and P30 (MPN141, MPN142, and MPN453, respectively) localize to the terminal organelle and are required for gliding (5,(8)(9)(10), these proteins are also essential for cytadherence and attachment to surfaces.…”

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confidence: 99%

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Protein Kinase/Phosphatase Function Correlates with Gliding Motility in Mycoplasma pneumoniae

Page

Krause

2013

J Bacteriol

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Mycoplasma pneumoniae exhibits a novel form of gliding motility that is mediated by the terminal organelle, a differentiated polar structure. Given that genes known to be involved in gliding in other organisms are absent in M. pneumoniae, random transposon mutagenesis was employed to generate mutants with gliding-deficient phenotypes. Transposon insertions in the only annotated Ser/Thr protein kinase gene (prkC; MPN248) and its cognate phosphatase gene (prpC; MPN247) in M. pneumoniae resulted in significant and contrasting effects on gliding frequencies. prkC mutant cells glided at approximately half the frequency of wild-type cells, while prpC mutant cells glided more than twice as frequently as wild-type cells. Phosphoprotein staining confirmed the association between phosphorylation of the cytoskeletal proteins HMW1 and HMW2 and membrane protein P1 and the gliding phenotype. When the prpC mutant was complemented by transposon delivery of a wild-type copy of the prpC allele, gliding frequencies and phosphorylation levels returned to the wild-type standard. Surprisingly, delivery of the recombinant wild-type prkC allele dramatically increased gliding frequency to a level approximately 3-fold greater than that of wild-type in the prkC mutant. Collectively, these data suggest that PrkC and PrpC work in opposition in M. pneumoniae to influence gliding frequency.M ycoplasma pneumoniae is a cell wall-less bacterial pathogen of the human respiratory tract causing primary atypical pneumonia and tracheobronchitis (1). Mycoplasmas lack major biosynthetic pathways, classical transcriptional regulators, chemotactic and other two-component systems, and the prototypical prokaryotic cell division apparatus (2, 3). The limited biosynthetic capabilities of mycoplasmas are generally explained by their evolution as obligate parasites of diverse eukaryotic hosts (4). Colonization of the host respiratory epithelium by M. pneumoniae requires gliding motility (5), which might facilitate access to receptors on the host cell surface and subsequent lateral spread.The gliding apparatus of M. pneumoniae is a polar terminal structure (6) that also functions in cell division (7) and adhesion to host receptors (2, 5). While the cytoskeletal protein HMW1 (MPN447) and membrane proteins P1, B/C, and P30 (MPN141, MPN142, and MPN453, respectively) localize to the terminal organelle and are required for gliding (5,(8)(9)(10), these proteins are also essential for cytadherence and attachment to surfaces. Accordingly, their distinct functions in gliding motility are difficult to define by mutagenesis alone. Given that the M. pneumoniae genome exhibits no homology to elements of defined gliding mechanisms (2, 3), including those of other gliding mycoplasmas (11-14), it was necessary to perform saturating transposon mutagenesis in order to identify the components specific to gliding (15). Transposon insertions in the genes encoding the cytoskeletal proteins P41 and P65 (MPN311 and MPN309, respectively) (16), which are known to localize to the termina...

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Protein P200 Is Dispensable for Mycoplasma pneumoniae Hemadsorption but Not Gliding Motility or Colonization of Differentiated Bronchial Epithelium

Cited by 51 publications

References 37 publications

First identification of proteins involved in motility of Mycoplasma gallisepticum

First identification of proteins involved in motility of Mycoplasma gallisepticum

Attachment organelle ultrastructure correlates with phylogeny, not gliding motility properties, in Mycoplasma pneumoniae relatives

Protein Kinase/Phosphatase Function Correlates with Gliding Motility in Mycoplasma pneumoniae

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