ArticleJournal of bacteriology2004
Use of fluorescent-protein tagging to determine the subcellular localization of mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
43 citing papers in PubMed, 77 citations in OpenAlex.
- Assembly Formation of P65 Protein, Featured by an Intrinsically Disordered Region Involved in Gliding Machinery ofBiomolecules · 2025Article
- Reviewing advancement inFrontiers in microbiology · 2024Review
- Gene editing tools for mycoplasmas: references and future directions for efficient genome manipulation.Frontiers in microbiology · 2023Review
- Genetic Manipulation of Mycoplasma pneumoniae.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Imaging Minimal Bacteria at the Nanoscale: a Reliable and Versatile Process to Perform Single-Molecule Localization Microscopy in Mycoplasmas.Microbiology spectrum · 2022Article
- Molecular ruler of the attachment organelle in Mycoplasma pneumoniae.PLoS pathogens · 2021Article
- Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile.Scientific reports · 2020Article
- Pathogenic Analysis of the Bronchoalveolar Lavage Fluid Samples With Pediatric RefractoryFrontiers in cellular and infection microbiology · 2020Article
- Behaviors and Energy Source ofJournal of bacteriology · 2019Article
- Mycoplasma pneumoniae from the Respiratory Tract and Beyond.Clinical microbiology reviews · 2017Review
- Structural Study of MPN387, an Essential Protein for Gliding Motility of a Human-Pathogenic Bacterium, Mycoplasma pneumoniae.Journal of bacteriology · 2016Article
- Article
- 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
- A Compendium for Mycoplasma pneumoniae.Frontiers in microbiology · 2016Review
- Systematic Structural Analyses of Attachment Organelle in Mycoplasma pneumoniae.PLoS pathogens · 2015Article
- A major determinant for gliding motility in Mycoplasma genitalium: the interaction between the terminal organelle proteins MG200 and MG491.The Journal of biological chemistry · 2015Article
- Cytadherence of Mycoplasma pneumoniae induces inflammatory responses through autophagy and toll-like receptor 4.Infection and immunity · 2014Article
- Localization of P42 and F(1)-ATPase α-subunit homolog of the gliding machinery in Mycoplasma mobile revealed by newly developed gene manipulation and fluorescent protein tagging.Journal of bacteriology · 2014Article
- Protein kinase/phosphatase function correlates with gliding motility in Mycoplasma pneumoniae.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma pneumoniae lacks a cell wall but has internal cytoskeleton-like structures that are assumed to support the attachment organelle and asymmetric cell shape of this bacterium. To explore the fine details of the attachment organelle and the cytoskeleton-like structures, a fluorescent-protein tagging technique was applied to visualize the protein components of these structures. The focus was on the four proteins--P65, HMW2, P41, and P24--that are encoded in the crl operon (for "cytadherence regulatory locus"), which is known to be essential for the adherence of M. pneumoniae to host cells. When the P65 and HMW2 proteins were fused to enhanced yellow fluorescent protein (EYFP), a variant of green fluorescent protein, the fused proteins became localized at the attachment organelle, enabling visualization of the organelles of living cells by fluorescence microscopy. The leading end of gliding M. pneumoniae cells, expressing the EYFP-P65 fusion, was observed as a focus of fluorescence. On the other hand, when the P41 and P24 proteins were labeled with EYFP, the fluorescence signals of these proteins were observed at the proximal end of the attachment organelle. Coexpression of the P65 protein labeled with enhanced cyan fluorescent protein clearly showed that the sites of localization of P41 and P24 did not overlap that of P65. The localization of P41 and P24 suggested that they are also cytoskeletal proteins that function in the formation of unknown structures at the proximal end of the attachment organelle. The fluorescent-protein fusion technique may serve as a powerful tool for identifying components of cytoskeleton-like structures and the attachment organelle. It can also be used to analyze their assembly.
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