The gene mpn310 (hmw2) from Mycoplasma pneumoniae encodes two proteins, HMW2 and HMW2-s, which differ in size but use the same reading frame

Boonmee, Atcha; Ruppert, Thomas; Herrmann, Richard

doi:10.1111/j.1574-6968.2008.01422.x

Cited by 7 publications

(5 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The Western blotting analyses showed the major bands at the positions close to those of 245 and 249 kDa expected from the amino acid sequences, respectively for the N-terminal and C-terminal fusions. The internal translation product corresponding to amino acids 1620–1818 of HMW2, designated as P28 was also detected near the expected gel position with the relative protein amount to HMW2 consistent with the previous study [ 40 , 41 ]. These results suggest that the fusion proteins were expressed and incorporated into the organelle in manners similar to those of the original HMW2 and P28, because the signals were not detected in additional positions.…”

Section: Resultssupporting

confidence: 90%

Systematic Structural Analyses of Attachment Organelle in Mycoplasma pneumoniae

et al. 2015

View full text Add to dashboard Cite

Mycoplasma pneumoniae, a human pathogenic bacterium, glides on host cell surfaces by a unique and unknown mechanism. It forms an attachment organelle at a cell pole as a membrane protrusion composed of surface and internal structures, with a highly organized architecture. In the present study, we succeeded in isolating the internal structure of the organelle by sucrose-gradient centrifugation. The negative-staining electron microscopy clarified the details and dimensions of the internal structure, which is composed of terminal button, paired plates, and bowl complex from the end of cell front. Peptide mass fingerprinting of the structure suggested 25 novel components for the organelle, and 3 of them were suggested for their involvement in the structure through their subcellular localization determined by enhanced yellow fluorescent protein (EYFP) tagging. Thirteen component proteins including the previously reported ones were mapped on the organelle systematically for the first time, in nanometer order by EYFP tagging and immunoelectron microscopy. Two, three, and six specific proteins localized specifically to the terminal button, the paired plates, and the bowl, respectively and interestingly, HMW2 molecules were aligned parallel to form the plate. The integration of these results gave the whole image of the organelle and allowed us to discuss possible gliding mechanisms.

show abstract

Section: Resultssupporting

confidence: 90%

Systematic Structural Analyses of Attachment Organelle in Mycoplasma pneumoniae

et al. 2015

View full text Add to dashboard Cite

show abstract

“…2B). MG218Ct is a 28 kDa polypeptide corresponding to the C-term region of MG218 coded by a small open reading frame (ORF) located at the 3 0 end of MG_218 gene (Boonmee et al, 2009;Broto, unpublished). MG217 protein homologous to M. pneumoniae P65 is located, together with MG317 and P32, at the distal end of the tip structure (Baseman et al, 1987;Jordan et al, 2001;Kenri et al, 2004;Hasselbring and Krause, 2007a;Burgos et al, 2008).…”

Section: Resultsmentioning

confidence: 99%

A minimized motile machinery for Mycoplasma genitalium

Garcia-Morales

González-González

Querol

et al. 2016

Molecular Microbiology

View full text Add to dashboard Cite

SummaryThe cell wall-less bacterium Mycoplasma genitalium uses specialized adhesins located at the terminal organelle to adhere to host cells and surfaces. The terminal organelle is a polar structure protruding from the cell body that is internally supported by a cytoskeleton and also has an important role in cell motility. We have engineered a M. genitalium null mutant for MG491 protein showing a massive downstream destabilization of proteins involved in the terminal organelle organization. This mutant strain exhibited striking similarities with the previously isolated MG_218 null mutant strain. Upon introduction of an extra copy of MG_318 gene in both strains, the amount of main adhesins P140 and P110 dramatically increased. These strains were characterized by microcinematography, epifluorescence microscopy and cryo-electron microcopy, revealing the presence of motile cells and filaments in the absence of many proteins considered essential for cell adhesion and motility. These results indicate that adhesin complexes play a major role in the motile machinery of M. genitalium and demonstrate that the rod element of the cytoskeleton core is not the molecular motor propelling mycoplasma cells. These strains containing a minimized motile machinery also provide a valuable cell model to investigate the adhesion and gliding properties of this human pathogen.

show abstract

“…Parallel to the thick plate is the thin plate, which contains HMW1 (118). Adjacent to the plates at the end close to the cell body, and likely in contact with the chromosomal DNA (128), is the bowl complex, which contains proteins P200, TopJ, P41, and P24 and a protein that arises from an internal translational start within the gene coding for HMW2, called P28 or HMW2-S (118,474). The bowl complex may be in contact with the membrane.…”

Section: Other Virulence Factorsmentioning

confidence: 99%

Mycoplasma pneumoniae from the Respiratory Tract and Beyond

et al. 2017

View full text Add to dashboard Cite

is an important cause of respiratory tract infections in children as well as adults that can range in severity from mild to life-threatening. Over the past several years there has been much new information published concerning infections caused by this organism. New molecular-based tests for detection are now commercially available in the United States, and advances in molecular typing systems have enhanced understanding of the epidemiology of infections. More strains have had their entire genome sequences published, providing additional insights into pathogenic mechanisms. Clinically significant acquired macrolide resistance has emerged worldwide and is now complicating treatment. susceptibility testing methods have been standardized, and several new drugs that may be effective against this organism are undergoing development. This review focuses on the many new developments that have occurred over the past several years that enhance our understanding of this microbe, which is among the smallest bacterial pathogens but one of great clinical importance.

show abstract

The gene mpn310 (hmw2) from Mycoplasma pneumoniae encodes two proteins, HMW2 and HMW2-s, which differ in size but use the same reading frame

Cited by 7 publications

References 26 publications

Systematic Structural Analyses of Attachment Organelle in Mycoplasma pneumoniae

Systematic Structural Analyses of Attachment Organelle in Mycoplasma pneumoniae

A minimized motile machinery for Mycoplasma genitalium

Mycoplasma pneumoniae from the Respiratory Tract and Beyond

Contact Info

Product

Resources

About