Flavobacterium johnsoniae SprA is a cell surface protein involved in gliding motility.
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ABSTRACT:
SUBMITTER: Nelson SS
PROVIDER: S-EPMC2045224 | biostudies-literature | 2007 Oct
REPOSITORIES: biostudies-literature
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Flavobacterium johnsoniae SprA is a cell surface protein involved in gliding motility.
Nelson Shawn S SS Glocka Padden P PP Agarwal Sarika S Grimm David P DP McBride Mark J MJ
Journal of bacteriology 20070720 19
Flavobacterium johnsoniae cells glide rapidly over surfaces by an unknown mechanism. Transposon-induced sprA mutants formed nonspreading colonies on agar, and the cells examined in wet mounts were deficient in attachment to surfaces and were almost completely nonmotile. Exposure of intact cells to proteinase K cleaved the 270-kDa SprA into several large peptides, suggesting that it is partially exposed on the cell surface. ...[more]
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Project description:Flavobacterium johnsoniae exhibits rapid gliding motility over surfaces. At least 20 genes are involved in this process. Seven of these, gldK, gldL, gldM, gldN, sprA, sprE, and sprT, encode proteins of the type IX protein secretion system (T9SS). The T9SS is required for surface localization of the motility adhesins SprB and RemA, and for secretion of the soluble chitinase ChiA. Here, we demonstrate that the gliding motility proteins GldA, GldB, GldD, GldF, GldH, GldI, and GldJ are also essential for secretion. Cells with mutations in the genes encoding any of these seven proteins had normal levels of gldK mRNA but dramatically reduced levels of the GldK protein, which may explain the secretion defects of the motility mutants. GldJ is necessary for stable accumulation of GldK, and each mutant lacked the GldJ protein. F. johnsoniae cells that produced truncated GldJ, lacking eight to 13 amino acids from the C terminus, accumulated GldK but were deficient in gliding motility. SprB was secreted by these cells but was not propelled along their surfaces. This C-terminal region of GldJ is thus required for gliding motility but not for secretion. The identification of mutants that are defective for motility but competent for secretion begins to untangle the F. johnsoniae gliding motility machinery from the T9SS.IMPORTANCE Many members of the phylum Bacteroidetes secrete proteins using T9SSs. T9SSs appear to be confined to members of this phylum. Many of these bacteria also glide rapidly over surfaces using a motility machine that is also confined to the Bacteroidetes and appears to be intertwined with the T9SS. This study identifies F. johnsoniae proteins that are required for both T9SS function and gliding motility. It also provides an explanation for the link between secretion and gliding and identifies mutants with defects in motility but not secretion.
| S-EPMC5738736 | biostudies-literature
Project description:Cells of the gliding bacterium Flavobacterium johnsoniae move rapidly over surfaces by an unknown mechanism. Transposon insertions in sprB resulted in cells that were defective in gliding. SprB is a highly repetitive 669-kDa cell surface protein, and antibodies against SprB inhibited the motility of wild-type cells. Polystyrene microspheres coated with antibodies against SprB attached to and were rapidly propelled along the cell surface, suggesting that SprB is one of the outermost components of the motility machinery. The movement of SprB along the cell surface supports a model of gliding motility in which motors anchored to the cell wall rapidly propel cell surface adhesins.
| S-EPMC2293251 | biostudies-literature
Project description:Cells of Flavobacterium johnsoniae move rapidly over surfaces by a process known as gliding motility. Gld proteins are thought to comprise the motor that propels the cell surface adhesin SprB. Cells with mutations in sprB are partially defective in motility and are also resistant to some bacteriophages. Transposon mutagenesis of a strain carrying a deletion spanning sprB identified eight mutants that were resistant to additional phages and exhibited reduced motility. Four of the mutants had transposon insertions in remA, which encodes a cell surface protein that has a lectin domain and appears to interact with polysaccharides. Three other genes identified in this screen (remC, wza, and wzc) encode proteins predicted to be involved in polysaccharide synthesis and secretion. Myc-tagged versions of RemA localized to the cell surface and were propelled rapidly along the cell at speeds of 1 to 2 ?m/s. Deletion of gldN and gldO, which encode components of a bacteroidete protein secretion system, blocked the transport of RemA to the cell surface. Overexpression of RemA resulted in the formation of cell aggregates that were dispersed by the addition of galactose or rhamnose. Cells lacking RemC, Wza, and Wzc failed to aggregate. Cells of a remC mutant and cells of a remA mutant, neither of which formed aggregates in isolation, aggregated when they were mixed together, suggesting that polysaccharides secreted by one cell may interact with RemA on another cell. Fluorescently labeled lectin Ricinus communis agglutinin I detected polysaccharides secreted by F. johnsoniae. The polysaccharides bound to cells expressing RemA and were rapidly propelled on the cell surface. RemA appears to be a mobile cell surface adhesin, and secreted polysaccharides may interact with the lectin domain of RemA and enhance motility.
| S-EPMC3393505 | biostudies-literature
Project description:Cells of Flavobacterium johnsoniae glide rapidly over surfaces. The mechanism of F. johnsoniae gliding motility is not known. Eight gld genes required for gliding motility have been described. Disruption of any of these genes results in complete loss of gliding motility, deficiency in chitin utilization, and resistance to bacteriophages that infect wild-type cells. Two modified mariner transposons, HimarEm1 and HimarEm2, were constructed to allow the identification of additional motility genes. HimarEm1 and HimarEm2 each transposed in F. johnsoniae, and nonmotile mutants were identified and analyzed. Four novel motility genes, gldK, gldL, gldM, and gldN, were identified. GldK is similar in sequence to the lipoprotein GldJ, which is required for gliding. GldL, GldM, and GldN are not similar in sequence to proteins of known function. Cells with mutations in gldK, gldL, gldM, and gldN were defective in motility and chitin utilization and were resistant to bacteriophages that infect wild-type cells. Introduction of gldA, gldB, gldD, gldFG, gldH, gldI, and gldJ and the region spanning gldK, gldL, gldM, and gldN individually into 50 spontaneous and chemically induced nonmotile mutants restored motility to each of them, suggesting that few additional F. johnsoniae gld genes remain to be identified.
| S-EPMC1251627 | biostudies-literature
Project description:UnlabelledGliding motility is common in members of the phylum Bacteroidetes, including Flavobacterium johnsoniae and Cellulophaga algicola. F. johnsoniae gliding has been extensively studied and involves rapid movement of the cell surface adhesin SprB. Genetic analysis of C. algicola allowed a comparative analysis of gliding. Sixty-three HimarEm1-induced mutants that formed nonspreading colonies were characterized. Each had an insertion in an ortholog of an F. johnsoniae motility gene, highlighting similarities between the motility systems. Differences were also observed. C. algicola lacks orthologs of the F. johnsoniae motility genes gldA, gldF, and gldG that are thought to encode the components of an ATP-binding cassette (ABC) transporter. In addition, mutations in any of 12 F. johnsoniae gld genes result in complete loss of motility, whereas all C. algicola gld mutants retained slight residual motility. This may indicate that C. algicola has multiple motility systems, that the motility proteins exhibit partial redundancy of function, or that essential components of the motility machinery of both C. algicola and F. johnsoniae remain to be discovered.ImportanceThe development of genetic tools for C. algicola and comparative analysis of F. johnsoniae and C. algicola motility mutants identified similarities and differences between their gliding motility machineries. Gliding motility is common in the phylum Bacteroidetes Proteins that are important for gliding in both C. algicola and F. johnsoniae are potential core components of the Bacteroidetes gliding motility machinery.
| S-EPMC4886757 | biostudies-literature
Project description:Cells of the gliding bacterium Flavobacterium johnsoniae move rapidly over surfaces. Transposon mutagenesis was used to identify sprE, which is involved in gliding. Mutations in sprE resulted in the formation of nonspreading colonies on agar. sprE mutant cells in wet mounts were almost completely deficient in attachment to and movement on glass, but a small percentage of cells exhibited slight movements, indicating that the motility machinery was not completely disrupted. SprE is a predicted lipoprotein with a tetratricopeptide repeat domain. SprE is similar in sequence to Porphyromonas gingivalis PorW, which is required for secretion of gingipain protease virulence factors. Disruption of F. johnsoniae sprE resulted in decreased extracellular chitinase activity and decreased secretion of the cell surface motility protein SprB. Reduced secretion of cell surface components of the gliding machinery, such as SprB, may account for the defects in gliding. Orthologs of sprE are found in many gliding and nongliding members of the phylum Bacteroidetes, suggesting that similar protein secretion systems are common among members of this large and diverse group of bacteria.
| S-EPMC3187464 | biostudies-literature
Project description:Flavobacterium johnsoniae is a gram-negative bacterium that exhibits gliding motility. To determine the mechanism of flavobacterial gliding motility, we isolated 33 nongliding mutants by Tn4351 mutagenesis. Seventeen of these mutants exhibited filamentous cell morphology. The region of DNA surrounding the transposon insertion in the filamentous mutant CJ101-207 was cloned and sequenced. The transposon was inserted in a gene that was similar to Escherichia coli ftsX. Two of the remaining 16 filamentous mutants also carried insertions in ftsX. Introduction of the wild-type F. johnsoniae ftsX gene restored motility and normal cell morphology to each of the three ftsX mutants. CJ101-207 appears to be blocked at a late stage of cell division, since the filaments produced cross walls but cells failed to separate. In E. coli, FtsX is thought to function with FtsE in translocating proteins involved in potassium transport, and perhaps proteins involved in cell division, into the cytoplasmic membrane. Mutations in F. johnsoniae ftsX may prevent translocation of proteins involved in cell division and proteins involved in gliding motility into the cytoplasmic membrane, thus resulting in defects in both processes. Alternatively, the loss of gliding motility may be an indirect result of the defect in cell division. The inability to complete cell division may alter the cell architecture and disrupt gliding motility by preventing the synthesis, assembly, or functioning of the motility apparatus.
| S-EPMC94465 | biostudies-literature
Project description:Cells of Flavobacterium johnsoniae glide rapidly over surfaces by an unknown mechanism. Eight genes required for gliding motility have been described. Complementation of the nonmotile mutant UW102-48 identified another gene, gldJ, that is required for gliding. gldJ mutants formed nonspreading colonies, and individual cells were completely nonmotile. Like previously described nonmotile mutants, gldJ mutants were deficient in chitin utilization and were resistant to bacteriophages that infect wild-type cells. Cell fractionation and labeling studies with [(3)H]palmitate indicated that GldJ is a lipoprotein. Mutations in gldA, gldB, gldD, gldF, gldG, gldH, or gldI resulted in normal levels of gldJ transcript but decreased levels of GldJ protein. Expression of truncated GldJ protein in wild-type cells resulted in a severe motility defect. GldJ was found in regular bands that suggest the presence of a helical structure within the cell envelope.
| S-EPMC1070399 | biostudies-literature
Project description:Flavobacterium johnsoniae cells glide rapidly over surfaces by an as-yet-unknown mechanism. Using cryo-electron tomography, we show that wild-type cells display tufts of approximately 5-nm-wide cell surface filaments that appear to be anchored to the inner surface of the outer membrane. These filaments are absent in cells of a nonmotile gldF mutant but are restored upon expression of plasmid-encoded GldF, a component of a putative ATP-binding cassette transporter.
| S-EPMC2168446 | biostudies-literature
Project description:Cells of Flavobacterium johnsoniae move over surfaces by a process known as gliding motility. The mechanism of this form of motility is not known. Cells of F. johnsoniae propel latex spheres along their surfaces, which is thought to be a manifestation of the motility machinery. Three of the genes that are required for F. johnsoniae gliding motility, gldA, gldB, and ftsX, have recently been described. Tn4351 mutagenesis was used to identify another gene, gldD, that is needed for gliding. Tn4351-induced gldD mutants formed nonspreading colonies, and cells failed to glide. They also lacked the ability to propel latex spheres and were resistant to bacteriophages that infect wild-type cells. Introduction of wild-type gldD into the mutants restored motility, ability to propel latex spheres, and sensitivity to bacteriophage infection. gldD codes for a cytoplasmic membrane protein that does not exhibit strong sequence similarity to proteins of known function. gldE, which lies immediately upstream of gldD, encodes another cytoplasmic membrane protein that may be involved in gliding motility. Overexpression of gldE partially suppressed the motility defects of a gldB point mutant, suggesting that GldB and GldE may interact. GldE exhibits sequence similarity to Borrelia burgdorferi TlyC and Salmonella enterica serovar Typhimurium CorC.
| S-EPMC95305 | biostudies-literature