Mycoplasma adhesion

Razin, Shmuel; Jacobs, Enno

doi:10.1099/00221287-138-3-407

Cited by 232 publications

(225 citation statements)

References 26 publications

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“…6). This would enable the three different loops to form a triangular structure, which might exhibit a stronger adherence capacity due to cooperative binding to the receptor molecule Razin & Jacobs, 1992). However, the adhesion-mediating protein sequences might not be identical to the sequences described as immunogenic epitopes.…”

Section: Discussionmentioning

confidence: 99%

“…However, no inhibition is observed using antibodies that target the N-terminal parts of the proteins. In mycoplasma-free extracts, P1 binds to host cells, suggesting a direct role for P1 in host receptor binding (Krause, 1998;Razin & Jacobs, 1992). Thus, the anti-P1 antibody inhibition of adhesion could originate from blocking of the adhesion region of P1.…”

Section: Introductionmentioning

confidence: 99%

“…Adhering mycoplasmas contain several adhesins, and M. pneumoniae expresses at least three different adhesins, termed P1, P30 and P116, suggesting that there are multiple receptors for M. pneumoniae on the host cells (Razin & Jacobs, 1992;Svenstrup et al, 2002). Monospecific antibodies raised against P116 block the adhesion of M. pneumoniae to HEp-2 cells, as do antibodies against the P30 protein (Baseman et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

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Interaction between the P1 protein of Mycoplasma pneumoniae and receptors on HEp-2 cells

et al. 2007

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The human pathogen Mycoplasma pneumoniae can cause atypical pneumonia through adherence to epithelial cells in the respiratory tract. The major immunogenic protein, P1, participates in the attachment of the bacteria to the host cells. To investigate the adhesion properties of P1, a recombinant protein (rP1-II) covering amino acids 1107-1518 of the P1 protein was produced. This protein inhibited the adhesion of M. pneumoniae to human HEp-2 cells, as visualized in a competitive-binding assay using immunofluorescence microscopy. Previous studies have shown that mAbs that recognize two epitopes in this region of P1 also reduce M. pneumoniae adhesion. Therefore, peptides covering these epitopes, of 8 and 13 aa, respectively, were synthesized to further investigate the adhesion region. None of these synthetic peptides reduced the binding of M. pneumoniae to the receptors on the host cells. Instead, 10 overlapping synthetic peptides covering the whole of rP1-II were evaluated in the competitivebinding assay using immunofluorescence microscopy. A reduction in the number of M. pneumoniae microcolonies was seen, which was confirmed for five peptides using a POLARstar OPTIMA reader to measure fluorescence intensity. The number of M. pneumoniae microcolonies adhering to the host cells was significantly reduced by these five peptides. Further investigations showed that inhibiting peptide 7 (amino acids 1347-1396) of the major adhesin protein P1 bound directly to host receptors, suggesting that the observed M. pneumoniae-inhibiting peptides occupied HEp-2 receptors, which are otherwise available for P1-mediated M. pneumoniae adhesion.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Interaction between the P1 protein of Mycoplasma pneumoniae and receptors on HEp-2 cells

et al. 2007

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“…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.…”

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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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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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“…Cell asymmetry is related to the attachment organelle, a membrane-bound extension of the cell. The correct assembly of this organelle is a prerequisite for binding of M. pneumoniae to specific receptors on the host cell Razin & Jacobs, 1992). Among the proteins known to be present in an intact attachment organelle are the proposed adhesin proteins P1 (Hu et al, 1977 ;Inamine et al, 1988 ;Su et al, 1987) and P30 (Dallo et al, 1990 ;Romero-Arroyo et al, 1999), and a number of other proteins including P40 and P90, cleavage products derived from the ORF6 gene of the P1 operon (Inamine et al, 1988 ;Layh-Schmitt & Harkenthal, 1999 ;Sperker et al, 1991), and HMW3 (Ogle et al, 1991 ;Stevens & Krause, 1992).…”

Section: Introductionmentioning

confidence: 99%

Defining the mycoplasma ‘cytoskeleton’: the protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2-D gel electrophoresis and mass spectrometry

et al. 2001

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After treating Mycoplasma pneumoniae cells with the nonionic detergent Triton X-100, an undefined, structured protein complex remains that is called the ' Triton X-100 insoluble fraction ' or ' Triton shell '. By analogy with eukaryotic cells and supported by ultrastructural analyses it is supposed that this fraction contains the components of a bacterial cytoskeleton-like structure. In this study, the composition of the Triton X-100 insoluble fraction was defined by electron microscopic screening for possible structural elements, and by two-dimensional (2-D) gel electrophoresis and MS to identify the proteins present. Silver staining of 2-D gels revealed about 100 protein spots. By staining with colloidal Coomassie blue, about 50 protein spots were visualized, of which 41 were identified by determining the mass and partial sequence of tryptic peptides of individual proteins. The identified proteins belonged to several functional categories, mainly energy metabolism, translation and heat-shock response. In addition, lipoproteins were found and most of the proteins involved in cytadherence that were previously shown to be components of the Triton X-100 insoluble fraction. There were also 11 functionally unassigned proteins. Based on sequence-derived predictions, some of these might be potential candidates for structural components. Quantitatively, the most prevalent proteins were the heat-shock protein DnaK, elongation factor Tu and subunits α and β of the pyruvate dehydrogenase complex (PdhA, PdhB), but definite conclusions regarding the composition of the observed structures can only be drawn after specific proteins are assigned to them, for example by immunocytochemistry.

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Mycoplasma adhesion

Cited by 232 publications

References 26 publications

Interaction between the P1 protein of Mycoplasma pneumoniae and receptors on HEp-2 cells

Interaction between the P1 protein of Mycoplasma pneumoniae and receptors on HEp-2 cells

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

Defining the mycoplasma ‘cytoskeleton’: the protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2-D gel electrophoresis and mass spectrometry

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