ArticleJournal of bacteriology2001
Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 39 citations in OpenAlex.
- Immune dysregulation inFrontiers in immunology · 2026Review
- Electron cryotomography of Mycoplasma pneumoniae mutants correlates terminal organelle architectural features and function.Molecular microbiology · 2018Article
- Mycoplasma pneumoniae from the Respiratory Tract and Beyond.Clinical microbiology reviews · 2017Review
- Article
- 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
- Mycoplasma pneumoniae, an underutilized model for bacterial cell biology.Journal of bacteriology · 2014Review
- P65 truncation impacts P30 dynamics during Mycoplasma pneumoniae gliding.Journal of bacteriology · 2012Article
- Loss of co-chaperone TopJ impacts adhesin P1 presentation and terminal organelle maturation in Mycoplasma pneumoniae.Molecular microbiology · 2011Article
- Functional domain analysis of the Mycoplasma pneumoniae co-chaperone TopJ.Molecular microbiology · 2010Article
- Mycoplasma pneumoniae J-domain protein required for terminal organelle function.Molecular microbiology · 2009Article
- The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin.Infection and immunity · 2008Article
- 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
- Protein P200 is dispensable for Mycoplasma pneumoniae hemadsorption but not gliding motility or colonization of differentiated bronchial epithelium.Infection and immunity · 2007Article
- 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mycoplasma pneumoniae adsorbs to host respiratory epithelium primarily by its attachment organelle, the proper function of which depends upon mycoplasma adhesin and cytoskeletal proteins. Among the latter are the cytadherence-associated proteins HMW1 and HMW2, whose specific roles in this process are unknown. In the M. pneumoniae cytadherence mutant I-2, loss of HMW2 results in accelerated turnover of HMW1 and other cytadherence-accessory proteins, probably by proteolysis. However, both the mechanism of degradation and the means by which these proteins are rendered susceptible to it are not understood. In this study, we addressed whether HMW1 degradation is a function of its presence among specific subcellular fractions and established that HMW1 is a peripheral membrane protein that is antibody accessible on the outer surfaces of both wild-type and mutant I-2 M. pneumoniae but to a considerably lesser extent in the mutant. Quantitation of HMW1 in Triton X-100-fractionated extracts from cells pulse-labeled with [(35)S]methionine indicated that HMW1 is synthesized in a Triton X-100-soluble form that exists in equilibrium with an insoluble (cytoskeletal) form. Pulse-chase analysis demonstrated that over time, HMW1 becomes stabilized in the cytoskeletal fraction and associated with the cell surface in wild-type M. pneumoniae. The less efficient transition to the cytoskeleton and mycoplasma cell surface in mutant I-2 leads to accelerated degradation of HMW1. These data suggest a role for HMW2 in promoting export of HMW1 to the cell surface, where it is stable and fully functional.
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