ArticleJournal of bacteriology1995
The proline-rich P65 protein of Mycoplasma pneumoniae is a component of the Triton X-100-insoluble fraction and exhibits size polymorphism in the strains M129 and FH.
Article in Journal of bacteriology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 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
- Expression, Purification, Characterization and Cellular Uptake of MeCP2 Variants.The protein journal · 2022Article
- PRPs localized to the middle lamellae are required for cortical tissue integrity in Medicago truncatula roots.Plant molecular biology · 2020Article
- Cloning, Expression and Purification of Espc, Espb and Espc/Espb Proteins ofReports of biochemistry & molecular biology · 2020Article
- Mycoplasma pneumoniae, an underutilized model for bacterial cell biology.Journal of bacteriology · 2014Review
- Type 1 and type 2 strains of Mycoplasma pneumoniae form different biofilms.Microbiology (Reading, England) · 2013Article
- Construction and evaluation of a novel recombinant T cell epitope-based vaccine against Coccidioidomycosis.Infection and immunity · 2012Article
- P65 truncation impacts P30 dynamics during Mycoplasma pneumoniae gliding.Journal of bacteriology · 2012Article
- Insights into the function of Mycoplasma pneumoniae protein P30 from orthologous gene replacement.Microbiology (Reading, England) · 2011Article
- Successful expression and purification of DPPD using a codon optimized synthetic gene.Open journal of immunology · 2011Article
- Domain analysis of protein P30 in Mycoplasma pneumoniae cytadherence and gliding motility.Journal of bacteriology · 2011Article
- Article
- RGD motif of lipoprotein T, involved in adhesion of Mycoplasma conjunctivae to lamb synovial tissue cells.Journal of bacteriology · 2010Article
- Functional domain analysis of the Mycoplasma pneumoniae co-chaperone TopJ.Molecular microbiology · 2010Article
- Genomic analysis reveals Mycoplasma pneumoniae repetitive element 1-mediated recombination in a clinical isolate.Infection and immunity · 2008Article
- Culture-independent molecular subtyping of Mycoplasma pneumoniae in clinical samples.Journal of clinical microbiology · 2006Article
- Identification of fibronectin-binding proteins in Mycoplasma gallisepticum strain R.Infection and immunity · 2006Article
- A recombinant aspartyl protease of Coccidioides posadasii induces protection against pulmonary coccidioidomycosis in mice.Infection and immunity · 2006Article
- A metalloproteinase of Coccidioides posadasii contributes to evasion of host detection.Infection and immunity · 2005Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previously, we described the identification of a novel Mycoplasma pneumoniae M129 protein, named P65 because of its apparent molecular mass of 65 kDa estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (T. Proft and R. Herrmann, Mol. Microbiol. 13:337-348, 1994). DNA sequence analysis of the P65 open reading frame (orfp65), however, revealed an ORF encoding a protein with a molecular weight of 47,034. This discrepancy can be explained by the unusual amino acid composition of this protein. According to the deduced amino acid sequence, the N-terminal half of P65 contains several penta- and hexapeptides (DPNAY and DPNQAY) forming a proline-rich acidic domain. Secondary-structure predictions indicated beta-sheets and turns within that region, suggesting an extended and rigid conformation. Near the C terminus of P65 the tripeptide Arg-Gly-Asp (RGD) was found. This motif is known to play an important role in binding of extracellular matrix proteins to integrins. P65 could be located exclusively to the Triton X-100-insoluble cell fraction. The results of immunofluorescence microscopy and of immunoadsorption experiments indicated that P65 carries surface-exposed regions. Mild treatment of whole cells with proteases resulted in cleavage of a limited amount of P65 molecules, suggesting either that only a small percentage of P65 molecules are exposed on the surface or that protease cleavage is hampered by a compact protein conformation or by binding of an unknown component to P65. P65 exhibits size polymorphism in M. pneumoniae M129 and FH. This is caused by an intragenetic duplication of a 54-bp sequence within the FH orfp65. As a consequence, the number of DPNAY pentapeptides increased from 9 to 12 repeats in the FH strain.
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