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PubMed1998

Non-helical perturbations of the flagellar filament: Salmonella typhimurium SJW117 at 9.6 A resolution.

Using a liquid-helium-cooled superconducting electron cryo-microscope, we obtained low-dose images of negatively stained preparations at 4 K and collected structural data to 1/9.6 -1 for flagellar filaments from the strain SJW117 of Salmonella typhimurium (serotype gt). The subunits of this left-handed, straight filament are non-helically perturbed in a pairwise manner. The perturbation corresponds to an alternating conformation in every other row of subunits. These are the 5-start rows and, necessarily, the resulting structure has a seam. The perturbation is not confined to the outside but extends into the structure. We separated the non-symmetric and symmetric parts of the structural data and generated a three-dimensional reconstruction from the latter. The resulting density map is a structure similar in domain organization to the left-handed filament of S. typhimurium SJW1660. Filtered images generated from the non-symmetric component show an ordered and polar structure. The nature of the perturbation was analyzed by model building using a sphere to represent the subunit at low resolution. A lateral shift of approximately 10 degrees mimics the perturbation.

Flagella↗

PubMed1970

Structural properties and features of parasitic Bdellovibrio bacteriovorus.

The structure of five parasitic strains of Bdellovibrio bacteriovorus was studied by electron microscope after negative staining and in shadow-case and etched freeze-fractured preparations. Special attention was paid to the cell wall and the flagellar sheath which is continuous with the wall or part of it. These structural components reveal distinct features which are induced by certain staining substances; they are exceedingly susceptible to disruption by physical treatments, and in old cells often appear impaired. In freeze-fractured cells the wall shows characteristic fracturing tendencies not known in other microorganisms. These structural properties and features are distinct to Bdellovibrio wall and flagellar sheath, the structural integrity of which is a fundamental requirement for the infectivity and survival of this organism. The anterior end of Bdellovibrio is differentiated: 6 to 12 ring-like structures (9 to 12 nm, outer diameter) are built into its wall and several fibers (7 to 10 nm wide, up to 1.5 mum long) emerge from it. Intracellular structures, which are revealed as compact oval bodies bulging from the cell border and have internal laminated organization, are characteristic of Bdellovibrio after negative staining with certain compounds. These findings on the structure of parasitic Bdellovibrio substantiate previous observations indicating the uniqueness of this organism and add criteria for the identification of this genus.

Bacteria↗

PubMed1972

Flagellar assembly mutants in Escherichia coli.

Genetic and biochemical analysis of mutants defective in the synthesis of flagella in Escherichia coli revealed an unusual class of mutants. These mutants were found to produce short, curly, flagella-like filaments with low amplitude ( approximately 0.06 mum). The filaments were connected to characteristic flagellar basal caps and extended for 1 to 2 mum from the bacterial surface. The mutations in these strains were all members of one complementation group, group E, which is located between his and uvrC. The structural, serological, and chemical properties of the filament derived from the mutants closely resemble those of the flagellar hook structure. On the basis of these properties, it is suggested that these filaments are "polyhooks", i.e., repeated end-to-end polymers of the hook portion of the flagellum. Polyhooks are presumed to be the result of a defective cistron which normally functions to control the length of the hook region of the flagellum.

Alkanesulfonates↗

PubMed1983

Ultrastructure of the dinoflagellate Polykrikos. II. The nucleus and its connections to the flagellar apparatus.

Electron microscopy of the colonial dinoflagellate Polykrikos kofoidi revealed a nuclear cortex formed of two electron-dense cortical layers directly beneath the nuclear envelope. Nuclear pores were confined to vesicular outpocketings of the nuclear envelope over circular discontinuities in the cortical layers. A conspicuous fibrous ribbon extended from the nucleus to the flagellar apparatus of each zooid. The ribbons resembled in their structure and position the attractophores of termite flagellates. Each flagellar apparatus consisted of two flagella, two elongate axial kinetosomes, an oblique kinetosome, and two roots of markedly different periodicities.

Animals↗

PubMed1989

Wheat germ agglutinin induces mating reactions in Chlamydomonas eugametos by cross-linking agglutinin-associated glycoproteins in the flagellar membrane.

Species-specific binding between the flagellar surfaces of mating types plus and minus (mt+ and mt-) gametes of Chlamydomonas eugametos is mediated by mating type-specific agglutinins. Their interaction triggers several mating responses that are necessary for cell fusion, such as flagellar twitching, flagellar tip activation, redistribution of agglutinin molecules to the flagellar tip (tipping), and mating structure activation. Earlier, we reported that a monoclonal antibody (mAb 66.3) can induce mating reactions by cross-linking the agglutinins (Homan, W. L., A. Musgrave, H. de Nobel, R. Wagter, A. H. J. Kolk, D. de Wit, and H. van den Ende. 1988. J. Cell Biol. 107:177-189). Here we report that the lectin wheat germ agglutinin (WGA), which does not bind to the agglutinins, can also invoke all these mating reactions. We show, by immunofluorescence studies using anti-WGA and an agglutinin-specific monoclonal antibody (mAb 66.3), that WGA induces the redistribution of agglutinin to the flagellar tips of mt- gametes. Vice versa, when agglutinin tipping is induced by mAb 66.3, the WGA-binding glycoproteins are also tipped. Under the same conditions, the major flagellar glycoproteins are not redistributed, indicating that membrane transport is limited to a few components. We conclude that each agglutinin is associated with a WGA-binding glycoprotein. When cells lacking agglutinin or cells possessing inactive agglutinins are treated with WGA, mating responses are again elicited. The data suggest that clustering of agglutinin-containing complexes results in the production of intracellular signals, such as cAMP, and the coupling of the complex to a force generating system. In nature, the complexes are clustered via the agglutinins, but artificially they can be clustered by lectins or antibodies directed against other proteins in the complex.

Cell Membrane↗

PubMed1996

Structural and phylogenetic analysis of the MotA and MotB families of bacterial flagellar motor proteins.

MotA and MotB are two well-characterized proteins in Escherichia coli which are believed to function as the proton channel and the anchor, respectively, of the motor component of the bacterial flagellum. We have identified and analysed all currently sequenced members of the MotA and MotB families. Members of these families include (1) these E. coli proteins, (2) their pmf-interacting motor homologues in other bacteria, (3) two ORFs which map downstream of the gene encoding the catabolite repression-mediating CepA protein in Bacillus species and (4) unidentified open reading frames. With one exception (the MotB protein of Rhodobactec sphaeroides), members of the MotB family exhibit a C-terminal domain that is homologous to peptidoglycan-interaction domains of numerous sequenced lipoproteins and outer membrane proteins. Multiple alignments, average hydropathy and similarity plots, and phylogenetic trees have allowed (1) identification of regions of relative conservation, (2) definition of signature sequences for these protein families and (3) determination of relative phylogenetic distances relating all members of each family. The phylogenies of these proteins do not follow those of the organisms from which they were isolated, suggesting the presence of divergent isoforms in many bacteria. Phylogenetic analyses of the peptidoglycan-interaction domains of MotB proteins indicated that, except for MotB of R. sphaeroides, these domains became associated with the MotB proteins early during evolutionary history, before members of the MotB family or members of the outer membrane protein family diverged from each other.

Amino Acid Sequence↗

PubMed1975

[Ultrastructural observations on amastigote forms of Leishmania donovani in a case of laryngeal leishmaniasis].

An ultrastructural study on the amastigote stage of Leishmania donovani, in a rare case of laringeal involvement, was carried out. Many details of the fine morphology of this protozoon were observed under the electron microscope, i.e.: the outer membrane of host origin, periplast, subpellicular microtubules, kinetoplast, flagellum, flagellar pocket, multivesicular bodies. A presence of a new organelle (4 microtubules structure close to and running parallel to the flagellar pocket), previously not described in Leishmania donovani's species, was demonstrated in this indigenous strain (from Central Italy). The Authors found a limited number of subpellicular microtubules in this strain, i.e.: 72 microtubules. Differences in size and number of microtubules between strains must be investigated in more rigorous morphometric studies. It's possible that the number of the subpellicular microtubules represents a new taxonomic character.

Humans↗

PubMed1995

How bacteria sense and swim.

Cells of Escherichia coli or Salmonella typhimurium can sense chemicals in their environment and respond by moving toward some and away from others. The ability to sense and swim requires the products of approximately 50 genes, about 10 for detecting and processing sensory cues and the rest for assembly and operation of the flagella. The function of each component in the chemosensory signaling pathway is well understood. Signaling is known to involve phosphorylation of a set of cytoplasmic proteins, but questions remain concerning the protein conformational changes and interactions that take place. Functions have been assigned to almost all of the approximately 40 flagellar proteins, and the sequence of events in flagellar assembly has been largely determined. Flagellar assembly depends on a specialized apparatus for exporting certain flagellar components to their appropriate locations. The structure and mechanism of this apparatus remain a mystery, as does the mechanism by which the flagellar motor generates torque.

Chemotaxis↗

PubMed1993

Flagellar regeneration in Chlamydomonas: a model system for studying organelle assembly.

How do the many different components of an organelle assemble into a functional structure at an appropriate place and time? Flagellar regeneration by the biflagellate green alga Chlamydomonas is one experimental system in which genetics, biochemistry and ultrastructural analysis are being combined to investigate the assembly of a microtubule-containing organelle. Recent advances in the molecular biology of this 'green yeast' have made possible several new approaches to the problem of flagellar assembly; insights from these new approaches are the focus of this review.

Journal Article↗

PubMed1993

Identification of structures containing polyphosphate in Helicobacter pylori.

For the first time polyphosphate (poly P) granules have been detected in Helicobacter pylori organisms colonizing the gastric antrum as well as in organisms isolated from the same tissue. Poly P granules showed typical sublimation characteristics during exposure to the electron beam and chipped out of ultrathin sectioning. A prominent phosphorus signal was identified using elemental specific electron microscopy such as electron energy loss spectroscopy (EELS) and was localized to at least three different locations: the cytoplasm, the flagellar pole and in association with the cell membrane. Intracytoplasmatic structures had a diameter of 0.05-0.2 micron, whereas the structures near the flagellar pole were much smaller (0.02 micron). The membrane-associated phosphate aggregates were visible only after staining with Pb(NO3)2 or with electron spectroscopic imaging (ESI). Poly P granules seem to be important energy and phosphorus stores and it is thought that they participate in the regulation of various and distinct metabolic processes of H. pylori.

Cell Membrane↗

PubMed1998

Helical perturbations of the flagellar filament: rhizobium lupini H13-3 at 13 A resolution

Flagellar filaments are highly conserved structures in terms of the underlying symmetry of the polymer, subunit domain organization of the flagellin monomer, amino acid composition and primary sequence at the N and C termini. Traditionally, filaments are classified as "plain" or "complex." In complex filaments, the helical lattice is perturbed in a pairwise manner such that the symmetry is reduced along the 6-start helical lines. Both plain (unperturbed) and complex (helically perturbed) components are helically symmetric and share a common lattice. The perturbation in Rhizobium lupini H13-3 results in a subunit composed of a dimer of flagellin. We have generated a approximately 13 A resolution three-dimensional density map of the complex filament of R. lupini H13-3 from low-dose images of negatively stained filaments. Compared to a previous map, which extended to only approximately 25 A resolution and which was generated from only five filaments containing six layer-lines each, the current map is a product of merging 139 data sets containing 66 layer-lines each. The higher resolution and improved signal-to-noise yield a detailed and interpretable density map. The density map is divided into four concentric rings. These amount to two dense cylinders interconnected by low density radial spokes and wrapped by a three-start external winding. The unperturbed component of the map is strikingly similar to the known plain filament maps and, in particular, to that of Caulobacter crescentus. The helically perturbed component contributes mainly to the filaments's exterior (domain D3) where it comprises the tips of the outer domains interconnecting, pairwise, along the 11-start protofilaments and, again, laterally along the 6-start lines forming vertical and horizontal loops. Strong intersubunit connectivity occurs in the D2 shell and in the inner shell which is dominated by 3-start densities. The contribution of the complex component to the radial spokes seems negligible. Copyright 1998 Academic Press.

Journal Article↗

PubMed1981

Flagellar beat patterns and their possible evolution.

The roles of flagella and their functioning in unicellular organisms of various groups are described. Water propelled around a cell by the flagellum may cause locomotion of the cell and may bring near to the cell food particles that can be filtered from the water and phagocytosed. For purpose of locomotion alone, a relatively simple flagellar activity is adequate, but the efficient collection of particulate food requires modification of the flagellar activity or of the cell organization or both. The most sophisticated flagellar mechanisms are best explained as having been evolved for the collection of particulate food, although they may occur in groups that are now predominantly or entirely autotrophic. This is consistent with the view that heterotrophic flagellates requiring efficient particle collection for feeding evolved divergent flagellar mechanisms, based upon various structural patterns, and that only later did some of these divergent groups acquire their own particular types of plastid, presumably following phagotrophic uptake of the appropriate type of photosynthetic prokaryote and the establishment of a symbiotic association.

Animals↗

PubMed1996

Axonemal dyneins: assembly, organization, and regulation.

Progress in the sequence determination of dynein subunits is providing new insights into the locations of functional domains in these microtubule motors. Combined structural and biochemical analyses of flagellar mutations are also yielding information on the three-dimensional organization of the dynein arms and on the different components that target dynein arm assembly. Physiological approaches are revealing multiple pathways that regulate dynein activity.

Axons↗

PubMed1998

Cyclic nucleotide-gated channels on the flagellum control Ca2+ entry into sperm.

Cyclic nucleotide-gated (CNG) channels are key elements of cGMP- and cAMP-signaling pathways in vertebrate photoreceptor cells and in olfactory sensory neurons, respectively. These channels form heterooligomeric complexes composed of at least two distinct subunits (alpha and beta). The alpha subunit of cone photoreceptors is also present in mammalian sperm. Here we identify one short and several long less abundant transcripts of beta subunits in testis. The alpha and beta subunits are expressed in a characteristic temporal and spatial pattern in sperm and precursor cells. In mature sperm, the alpha subunit is observed along the entire flagellum, whereas the short beta subunit is restricted to the principal piece of the flagellum. These findings suggest that different forms of CNG channels coexist in the flagellum. Confocal microscopy in conjunction with the Ca2+ indicator Fluo-3 shows that the CNG channels serve as a Ca2+ entry pathway that responds more sensitively to cGMP than to cAMP. Assuming that CNG channel subtypes differ in their Ca2+ permeability, dissimilar localization of alpha and beta subunits may give rise to a pattern of Ca2+ microdomains along the flagellum, thereby providing the structural basis for control of flagellar bending waves.

Amino Acid Sequence↗

PubMed1998

Detection of verotoxin-producing Escherichia coli O157:H7 by multiplex polymerase chain reaction.

We constructed primers for multiplex polymerase chain reaction (PCR) to detect verotoxin-producing Escherichia coli (VTEC) O157:H7. The multiplex PCR primers were designed from the sequence of the flagellin structural gene of Escherichia coli flagellar type H7 (GenBank under accession number L07388), and from the sequence of the rfbE gene of Escherichia coli O157:H7 (GenBank under accession number S83460). In addition to these primers, we used a primer pair reported by Karch and Meyer (J. Clin. Microbiol. 27: 2751-2757, 1989) to amplify various VT genes from VTEC. All of the examined specimens (18 isolates) of VT-producing E. coli O157:H7 showed a positive result by the multiplex PCR test with the three sets of primers. The sensitivity of detection for VT-producing E. coli O157:H7 was shown to be at least 3,000 cells per PCR tube.

Animals↗

PubMed2006

The YfgL lipoprotein is essential for type III secretion system expression and virulence of Salmonella enterica Serovar Enteritidis.

Salmonella enterica, like many gram-negative pathogens, uses type three secretion systems (TTSS) to infect its hosts. The three TTSS of Salmonella, namely, TTSS-1, TTSS-2, and flagella, play a major role in the virulence of this bacterium, allowing it to cross the intestinal barrier and to disseminate systemically. Previous data from our laboratory have demonstrated the involvement of the chromosomal region harboring the yfgL, engA, and yfgJ open reading frames in S. enterica serovar Enteritidis virulence. Using microarray analysis and real-time reverse transcription-PCR after growth of bacterial cultures favorable for either TTSS-1 or TTSS-2 expression, we show in this study that the deletion in S. enterica serovar Enteritidis of yfgL, encoding an outer membrane lipoprotein, led to the transcriptional down-regulation of most Salmonella pathogenicity island 1 (SPI-1), SPI-2, and flagellar genes encoding the TTSS structural proteins and effector proteins secreted by these TTSS. In line with these results, the virulence of the DeltayfgL mutant was greatly attenuated in mice. Moreover, even if YfgL is involved in the assembly of outer membrane proteins, the regulation of TTSS expression observed was not due to an inability of the Delta yfgL mutant to assemble TTSS in its membrane. Indeed, when we forced the transcription of SPI-1 genes by constitutively expressing HilA, the secretion of the TTSS-1 effector protein SipA was restored in the culture supernatant of the mutant. These results highlight the crucial role of the outer membrane lipoprotein YfgL in the expression of all Salmonella TTSS and, thus, in the virulence of Salmonella. Therefore, this outer membrane protein seems to be a privileged target for fighting Salmonella.

Animals↗

PubMed1997

Putative channel components for the fast-rotating sodium-driven flagellar motor of a marine bacterium.

The polar flagellum of Vibrio alginolyticus rotates remarkably fast (up to 1,700 revolutions per second) by using a motor driven by sodium ions. Two genes, motX and motY, for the sodium-driven flagellar motor have been identified in marine bacteria, Vibrio parahaemolyticus and V. alginolyticus. They have no similarity to the genes for proton-driven motors, motA and motB, whose products constitute a proton channel. MotX was proposed to be a component of a sodium channel. Here we identified additional sodium motor genes, pomA and pomB, in V. alginolyticus. Unexpectedly, PomA and PomB have similarities to MotA and MotB, respectively, especially in the predicted transmembrane regions. These results suggest that PomA and PomB may be sodium-conducting channel components of the sodium-driven motor and that the motor part consists of the products of at least four genes, pomA, pomB, motX, and motY. Furthermore, swimming speed was controlled by the expression level of the pomA gene, suggesting that newly synthesized PomA proteins, which are components of a force-generating unit, were successively integrated into the defective motor complexes. These findings imply that Na+-driven flagellar motors may have similar structure and function as proton-driven motors, but with some interesting differences as well, and it is possible to compare and study the coupling mechanisms of the sodium and proton ion flux for the force generation.

Amino Acid Sequence↗

PubMed2001

Polar flagellar motility of the Vibrionaceae.

Polar flagella of Vibrio species can rotate at speeds as high as 100,000 rpm and effectively propel the bacteria in liquid as fast as 60 microm/s. The sodium motive force powers rotation of the filament, which acts as a propeller. The filament is complex, composed of multiple subunits, and sheathed by an extension of the cell outer membrane. The regulatory circuitry controlling expression of the polar flagellar genes of members of the Vibrionaceae is different from the peritrichous system of enteric bacteria or the polar system of Caulobacter crescentus. The scheme of gene control is also pertinent to other members of the gamma purple bacteria, in particular to Pseudomonas species. This review uses the framework of the polar flagellar system of Vibrio parahaemolyticus to provide a synthesis of what is known about polar motility systems of the Vibrionaceae. In addition to its propulsive role, the single polar flagellum of V. parahaemolyticus is believed to act as a tactile sensor controlling surface-induced gene expression. Under conditions that impede rotation of the polar flagellum, an alternate, lateral flagellar motility system is induced that enables movement through viscous environments and over surfaces. Although the dual flagellar systems possess no shared structural components and although distinct type III secretion systems direct the simultaneous placement and assembly of polar and lateral organelles, movement is coordinated by shared chemotaxis machinery.

Chemotaxis↗