ArticleJournal of bacteriology1992
Mycoplasma pneumoniae cytadherence phase-variable protein HMW3 is a component of the attachment organelle.
Article in Journal of bacteriology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 69 citations in OpenAlex.
- Imaging Minimal Bacteria at the Nanoscale: a Reliable and Versatile Process to Perform Single-Molecule Localization Microscopy in Mycoplasmas.Microbiology spectrum · 2022Article
- The clinical characteristics ofTranslational pediatrics · 2021Article
- Electron cryotomography of Mycoplasma pneumoniae mutants correlates terminal organelle architectural features and function.Molecular microbiology · 2018Article
- Structure-Guided Mutations in the Terminal Organelle Protein MG491 Cause Major Motility and Morphologic Alterations on Mycoplasma genitalium.PLoS pathogens · 2016Article
- Integrated Information and Prospects for Gliding Mechanism of the Pathogenic Bacterium Mycoplasma pneumoniae.Frontiers in microbiology · 2016Article
- Protein kinase/phosphatase function correlates with gliding motility in Mycoplasma pneumoniae.Journal of bacteriology · 2013Article
- Insights into the function of Mycoplasma pneumoniae protein P30 from orthologous gene replacement.Microbiology (Reading, England) · 2011Article
- Mycoplasma pneumoniae cytoskeletal protein HMW2 and the architecture of the terminal organelle.Journal of bacteriology · 2009Article
- Mycoplasma pneumoniae J-domain protein required for terminal organelle function.Molecular microbiology · 2009Article
- Functional analysis of the Mycoplasma genitalium MG312 protein reveals a specific requirement of the MG312 N-terminal domain for gliding motility.Journal of bacteriology · 2007Article
- Transposon mutagenesis identifies genes associated with Mycoplasma pneumoniae gliding motility.Journal of bacteriology · 2006Article
- Identification of fibronectin-binding proteins in Mycoplasma gallisepticum strain R.Infection and immunity · 2006Article
- HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae.Journal of bacteriology · 2004Article
- Attachment organelle formation represented by localization of cytadherence proteins and formation of the electron-dense core in wild-type and mutant strains of Mycoplasma pneumoniae.Journal of bacteriology · 2003Article
- Characterization of a Mycoplasma pneumoniae hmw3 mutant: implications for attachment organelle assembly.Journal of bacteriology · 2002Article
- Stability and subcellular localization of cytadherence-associated protein P65 in Mycoplasma pneumoniae.Journal of bacteriology · 2001Article
- Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell.Journal of bacteriology · 2001Article
- Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy.Journal of bacteriology · 2001Article
- Molecular characterization of the Mycoplasma gallisepticum pvpA gene which encodes a putative variable cytadhesin protein.Infection and immunity · 2000Article
- Transcriptional analysis of the hmw gene cluster of Mycoplasma pneumoniae.Journal of bacteriology · 1999Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The subcellular location of the phase-variable cytadherence-accessory protein HMW3 in Mycoplasma pneumoniae has been examined by biochemical and immunoelectron microscopic techniques. Analysis by Western blot (immunoblot) with HMW3-specific antiserum established the presence of this protein within the M. pneumoniae Triton X-100-insoluble fraction or triton shell. Immunogold labeling of Triton-extracted mycoplasmas with affinity-purified antibodies localized HMW3 to the terminal knob on the rodlike extensions of the triton shell, a location that would correspond to the adherence organelle in whole mycoplasmas. Treatment of triton shells with KI resulted in the selective removal of the adherence-accessory proteins HMW1 to HMW4. Analysis of these triton shells by transmission electron microscopy revealed dramatic ultrastructural changes in the filamentous network and core structure. Immunogold labeling of KI-extracted shells reflected the removal of HMW3 from the disrupted tip structure. An examination of ultrathin sections of wild-type cells by transmission electron microscopy following labeling with HMW3-specific antibodies provided further evidence for the nonrandom distribution of HMW3 and its localization to the terminal portion of filamentous cell extensions. Most colloidal gold molecules were associated with the cell interior, but limited peripheral labeling of the terminal region was also observed. Postfixation antibody labeling of whole cells suggested limited exposure of HMW3 on the mycoplasma surface at the tip structure. However, prefixation antibody labeling failed to indicate surface exposure, raising some uncertainty regarding the relationship of HMW3 with the mycoplasma membrane.
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