<i>Mycoplasma pneumoniae</i>
            Infection: Role of a Surface Protein in the Attachment Organelle

Hu, Ping; Cole, Roger M.; Huang, Yuan‐Shen; Graham, Judith A.; Gardner, Donald E.; Collier, Albert M.; Clyde, Wallace A.

doi:10.1126/science.6801766

Cited by 224 publications

(144 citation statements)

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“…To ensure optimal protease concentrations, antiserum against P1 protein and EF-G served as controls. P1 is the major adhesin of M. pneumoniae (3,25), and EF-G is a cytosolic protein. The control experiments showed that the proteinase K concentration used for the cleavage experiment is critical, since the range of protease concentration necessary for complete cleavage of P1 without affecting EF-G was very narrow (0.8 to 1.2 U/ml).…”

Section: Detection Of P65 In Triton X-100-insoluble Subfractionsmentioning

confidence: 99%

“…A critical step in bacterial colonization of the host cells is the specific adhesion to host cell receptors, mediated by bacterial adhesins. In M. pneumoniae, the P1 adhesin (3,17,25,26) and the adhesin-related 30-kDa protein (4, 10) have been identified. Both proteins are located mainly in a tip structure that functions as the attachment organelle of the bacterium.…”

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confidence: 99%

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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

et al. 1995

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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 ␤-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.Mycoplasma pneumoniae is an extracellular pathogen of the human respiratory tract (26, 46) causing histopathological changes of lung epithelial cells, usually in older children and young adults (18). A critical step in bacterial colonization of the host cells is the specific adhesion to host cell receptors, mediated by bacterial adhesins. In M. pneumoniae, the P1 adhesin (3,17,25,26) and the adhesin-related 30-kDa protein (4, 10) have been identified. Both proteins are located mainly in a tip structure that functions as the attachment organelle of the bacterium. It could be demonstrated, by nearestneighbor analysis with a hydrophilic chemical cross-linker, that the product of open reading frame 6 (ORF6) of the P1 operon (28), a 40-kDa protein and 90-kDa protein (9, 34, 50) are located in close proximity to the P1 adhesin on the cell surface (35).Scanning and transmission electron microscope analyses of M. pneumoniae cells grown on grids and pretreated with Triton X-100 revealed a rodlike tip structure and a network of filamentous strands (22,41). Krause and coworkers identified a set of high-molecular-weight proteins (HMW1 to HMW5) which play an important role in cytadherence (30,31,(51)(52)(53) and appear to be involved in formation of a cytoskeletonlike structure (38). These proteins, ...

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Section: Detection Of P65 In Triton X-100-insoluble Subfractionsmentioning

confidence: 99%

mentioning

confidence: 99%

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

et al. 1995

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“…The fibrillar element was well stained with ruthenium red, which specifically stains mucopolysaccharides. The second structure, observed by negative staining of M. pneumoniae, is a peplomer-like structure, called "nap" (1,10). The localization of nap is also restricted to the extracellular surface of the attachment organelle, similar to the distribution of spikes on the head-like protrusion of M. mobile.…”

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confidence: 98%

Spike Structure at the Interface between GlidingMycoplasma mobileCells and Glass Surfaces Visualized by Rapid-Freeze-and-Fracture Electron Microscopy

Miyata

Petersen

2004

J Bacteriol

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Mycoplasma mobile is a flask-shaped bacteria that binds to a substrate and glides towards its tapered end, the so-called "head-like protrusion," by an unknown mechanism. To search for cellular structures underlying this motility, the cell-substrate interface of actively gliding cells was visualized by rapid-freeze-and-freezefracture rotary-shadow electron microscopy. Novel structures, called "spikes," were observed to protrude from the cell membrane and attach to the glass surface at their distal end. The spikes were on average 50 nm in length and 4 nm in diameter, most abundant around the head, and not observed in a nonbinding mutant. The spikes may be involved in the mechanism of binding, gliding, or both.Mycoplasma gliding. Mycoplasmas are bacteria that lack a cell wall and are parasitic or commensal to many kinds of hosts, including humans, animals, and plants (25). Several mycoplasma species have a membrane protrusion at one end, called the "head-like protrusion," which creates the organism's characteristic flask-shaped cell morphology. These bacteria are capable of gliding motility, enabling them to translocate smoothly on solid surfaces, always in the direction of the headlike protrusion (3, 13). Although gliding motility of mycoplasmas is believed to be involved in pathogenicity, the mechanism of gliding motility has not been well investigated. Mycoplasmas do not have any homologs of genes that encode pili, flagella, genes related to other bacterial motility, or motor proteins that are common in eukaryotic motility, such as myosins (5,7,9,19). These facts suggest that mycoplasmas glide by an entirely unknown mechanism, but this mechanism has been difficult to isolate because many species of mycoplasma travel at low speed and with interrupted motility.The species Mycoplasma mobile provides an opportunity to study mycoplasma gliding motility, because this species is the fastest gliding and, unlike other species, glides without interruption (13-15, 20, 21, 27). At all stages of growth, M. mobile glides smoothly and continuously on glass at an average speed of 2.0 to 4.5 m/s, or about 3 to 7 times the length of the cell per s (27), exerting a force of up to 27 piconewtons (pN) (20,21). These distinct characteristics enabled detailed analyses of gliding (6,(20)(21)(22)(26)(27)(28) and isolation of gliding mutants that were characterized by reduced or deficient gliding or enhanced speed (23,28).

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“…The protein with the higher molecular mass, estimated at 170-190 kDa, was named P1 (Hu et al, 1977). Subsequent studies established that protein PI is the major adhesin of M. pneumoniae (Hu et al, 1982;Baseman et al, 1982;Feldner et al, 1982). M .…”

Section: The P1 Operon Genes and Proteinsmentioning

confidence: 99%

Mycoplasma adhesion

Razin¹,

Jacobs²

1992

Journal of General Microbiology

232

222

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Mycoplasma pneumoniae Infection: Role of a Surface Protein in the Attachment Organelle

Cited by 224 publications

References 10 publications

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

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

Spike Structure at the Interface between GlidingMycoplasma mobileCells and Glass Surfaces Visualized by Rapid-Freeze-and-Fracture Electron Microscopy

Mycoplasma adhesion

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