Cytoskeletal protein P41 is required to anchor the terminal organelle of the wall‐less prokaryote <i>Mycoplasma pneumoniae</i>

Hasselbring, Benjamin M.; Krause, Duncan C.

doi:10.1111/j.1365-2958.2006.05507.x

Cited by 51 publications

(74 citation statements)

References 34 publications

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“…In addition, the TO is the leading end as mycoplasma cells glide (Radestock & Bredt, 1977) and it constitutes the mycoplasma gliding motor (Hasselbring & Krause, 2007). Motility and cytadherence are closely related in mycoplasmas and many cytadherence-related proteins are also required for cell gliding (Burgos et al, 2007;Hasselbring et al, 2005;Hasselbring & Krause, 2007;Seto et al, 2005). However, the existence of a cytadherence-independent set of motility-related proteins has been disclosed recently for the slow gliding mycoplasmas M. genitalium (Pich et al, 2006a) and Mycoplasma pneumoniae (Hasselbring et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…Most of the cytoskeletal proteins present in the complex network that constitutes the TO have been identified primarily as cyadhesins or cytadherence-associated proteins. In addition, the TO is the leading end as mycoplasma cells glide (Radestock & Bredt, 1977) and it constitutes the mycoplasma gliding motor (Hasselbring & Krause, 2007). Motility and cytadherence are closely related in mycoplasmas and many cytadherence-related proteins are also required for cell gliding (Burgos et al, 2007;Hasselbring et al, 2005;Hasselbring & Krause, 2007;Seto et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence

et al. 2008

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The terminal organelle is a differentiated structure that plays a key role in mycoplasma cytadherence and locomotion. For this reason, the analysis of Mycoplasma genitalium mutants displaying anomalous terminal organelles could improve our knowledge regarding the structural elements required for proper locomotion. In this study, we isolated several M. genitalium mutants having transposon insertions within the mg218 or mg317 genes, which encode the orthologues of Mycoplasma pneumoniae HMW2 and HMW3 cytoskeletal proteins, respectively. As expected, mg218 " and mg317 " mutants exhibit a reduced gliding motility, although their ability to attach to solid surfaces was not completely abolished. Interestingly, most of the mg218 " mutants expressed N-terminal MG218 derivatives and showed the presence of short terminal organelles retaining many of the functions displayed by this structure in the wild-type strain, suggesting that the N-terminal region of this protein is an essential element in the architecture of the terminal organelle. Separately, the analysis of mg317 " mutants indicates that MG317 protein is involved in the formation of the terminal button and contributes to anchoring the electron-dense core to the cell membrane. The results presented here clearly show that MG218 and MG317 proteins are implicated in the maintenance of gliding motility and cytadherence in M. genitalium.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence

et al. 2008

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“…Electron micrographs of experimentally infected human and animal cells, as well as cells collected from natural M. pneumoniae infections, reveal an intimate relationship between this terminal organelle and the epithelial cell surface (7). The terminal organelle also mediates gliding motility (16,29), which may facilitate mycoplasma traversal of the airway surface liquid to allow access to host receptors on the apical surface of respiratory epithelium and refuge from the turbulent mucociliary escalator. …”

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

Jordan¹,

Chang²,

Balish³

et al. 2007

Infect Immun

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Mycoplasma pneumoniae protein P200 was localized to the terminal organelle, which functions in cytadherence and gliding motility. The loss of P200 had no impact on binding to erythrocytes and A549 cells but resulted in impaired gliding motility and colonization of differentiated bronchial epithelium. Thus, gliding may be necessary to overcome mucociliary clearance.Mycoplasma pneumoniae causes tracheobronchitis, bronchopneumonia, and a variety of extrapulmonary manifestations in humans (35). A distinct polar structure (5, 18) mediates host cell attachment (cytadherence) by this novel cell wall-less prokaryote. Electron micrographs of experimentally infected human and animal cells, as well as cells collected from natural M. pneumoniae infections, reveal an intimate relationship between this terminal organelle and the epithelial cell surface (7). The terminal organelle also mediates gliding motility (16,29), which may facilitate mycoplasma traversal of the airway surface liquid to allow access to host receptors on the apical surface of respiratory epithelium and refuge from the turbulent mucociliary escalator.

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“…It is noteworthy that the terminal organelle is also responsible for this movement (13), reinforcing the importance of this polar structure in mycoplasma pathogenesis. Many gliding motility proteins identified in M. pneumoniae (P1 and P30) and Mycoplasma mobile (Gli349, Gli521, and Gli123) appear also to be implicated in glass binding and hemadsorption (HA) (12,33,35,42,43), supporting the close relationship between the gliding motility and cytadherence machineries.…”

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Functional Analysis of the Mycoplasma genitalium MG312 Protein Reveals a Specific Requirement of the MG312 N-Terminal Domain for Gliding Motility

et al. 2007

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The human pathogen Mycoplasma genitalium is known to mediate cell adhesion to target cells by the attachment organelle, a complex structure also implicated in gliding motility. The gliding mechanism of M. genitalium cells is completely unknown, but recent studies have begun to elucidate the components of the gliding machinery. We report the study of MG312, a cytadherence-related protein containing in the N terminus a box enriched in aromatic and glycine residues (EAGR), which is also exclusively found in MG200 and MG386 gliding motility proteins. Characterization of an MG_312 deletion mutant obtained by homologous recombination has revealed that the MG312 protein is required for the assembly of the M. genitalium terminal organelle. This finding is consistent with the intermediate-cytadherence phenotype and the complete absence of gliding motility exhibited by this mutant. Reintroduction of several MG_312 deletion derivatives into the MG_312 null mutant allowed us to identify two separate functional domains: an N-terminal domain implicated in gliding motility and a C-terminal domain involved in cytadherence and terminal organelle assembly functions. In addition, our results also provide evidence that the EAGR box has a specific contribution to mycoplasma cell motion. Finally, the presence of a conserved ATP binding site known as a Walker A box in the MG312 N-terminal region suggests that this structural protein could also play an active function in the gliding mechanism.Mycoplasma genitalium is an important sexually transmitted pathogen capable of colonizing the human genitourinary tract. It is considered the principal causative agent of nonchlamydial, nongonococcal urethritis in men (18), and it has also been associated with genital tract diseases in women, such as endometritis (3), pelvic inflammatory disease, and cervicitis (7, 23). Furthermore, M. genitalium has been related to other extragenitourinary pathologies (40), including pneumonia, chronic fatigue, and arthritis. In addition to its clinical significance, M. genitalium has the smallest known genome among the organisms able to grow in axenic culture. In this sense, with just 525 genes (8, 9), this cell wall-less prokaryote is considered one of the most suitable models to understand the cellular biology of a self-replicating cell (30). Nonetheless, behind this apparent simplicity, a remarkable complexity exists, exemplified by the presence of a complex and differentiated polar structure, known as the attachment or terminal organelle. M. genitalium and several mycoplasma species accomplish surface adhesion by using this structure, which has been traditionally studied in Mycoplasma pneumoniae (21). The attachment organelle of M. pneumoniae is defined by the presence of an electron-dense core (15,16,36), and it is composed of a filamentous network of cytoskeletal proteins, including HMW1, HMW2, HMW3, B, C, P65, and the major cytadhesin P1 (29).M. genitalium cells have also the ability to locomote across solid surfaces by a novel and poorly characterized me...

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Cytoskeletal protein P41 is required to anchor the terminal organelle of the wall‐less prokaryote Mycoplasma pneumoniae

Cited by 51 publications

References 34 publications

Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence

Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence

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

Functional Analysis of the Mycoplasma genitalium MG312 Protein Reveals a Specific Requirement of the MG312 N-Terminal Domain for Gliding Motility

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