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PubMed2005

Phosphatase localization in bacterial chemotaxis: divergent mechanisms, convergent principles.

Chemotaxis is the process by which cells sense changes in their chemical environment and move towards more favorable conditions. In divergent species of bacteria, the chemotaxis proteins localize to the poles of the cell and information is transferred to the flagellar motors through the phosphorylation of a soluble protein CheY. Using mathematical models and computer simulation, we demonstrate that phosphatase localization controls the spatial distribution of CheY-P in the cytosol at steady state. Remarkably, the location of the phosphatase is not conserved in different species of bacteria. The sole phosphatase in Escherichia coli is localized with the signaling complex and the primary phosphatase in Bacillus subtilis is localized at the flagellar motors. Despite these alternate pathway structures, both designs minimize differences in the concentration of phosphorylated CheY proximal to each motor unlike a design where the phosphatase is freely diffusing in the cytoplasm. These results suggest that motile bacteria have evolved alternate mechanisms to ensure that each motor receives roughly the same signal at steady state. The hypothesis is that complex networks have evolved to satisfy certain design principles in order to function robustly. While specific mechanisms are different, the underlying principles of phosphatase localization in E. coli and B. subtilis appear to be the same.

Bacillus subtilis↗

PubMed2004

Effect of the lysophospholipid analogues edelfosine, ilmofosine and miltefosine against Leishmania amazonensis.

OBJECTIVES: Analysis of the effect of edelfosine, ilmofosine and miltefosine on Leishmania amazonensis and of potential targets of these lysophospholipid analogues. METHODS: Quantification and ultrastructural analysis of the effect of lysophospholipid analogues on promastigote forms and on infected peritoneal macrophages, and flow cytometry analysis of treated promastigotes labelled with propidium iodide and rhodamine 123 (Rh123). RESULTS: The lysophospholipid analogues presented potent antiproliferative activity with IC50/3 days of 1.9-3.4 microM for promastigotes and 4.2-9.0 microM for intracellular amastigotes. Treatment with these analogues in Schneider medium for 1 day led to a dose-dependent decrease in Rh123 fluorescence, an effect more accentuated in edelfosine-treated parasites, suggesting interference with the potential of the mitochondrial membrane. In both forms of L. amazonensis, edelfosine induced extensive mitochondrial damage, multinucleation and, in promastigotes, also led to plasma membrane alterations, formation of autophagic structures and membranous arrangements inside the flagellar pocket. CONCLUSIONS: The alkylglycerophosphocholines edelfosine and ilmofosine were more active than the alkylphosphocholine miltefosine against promastigotes and intracellular amastigotes of L. amazonensis, and ultrastructural and flow cytometry data indicate the mitochondrion as a target of edelfosine.

Animals↗

PubMed1996

Heterogeneity of Borrelia burgdorferi in the skin.

The reliability of various in vitro techniques to identify Borrelia burgdorferi infection is still unsatisfactory. Using a high-power resolution videomicroscope and staining with the borrelia genus-specific monoclonal flagellar antibody H9724, we identified borrelial structures in skin biopsies of erythema chronicum migrans (from which borrelia later was cultured), of acrodermatitis chronica atrophicans, and of morphea. In addition to typical borreliae, we noted stained structures of varying shapes identical to borreliae found in a "borrelia-injected skin" model; identical to agar-embedded borreliae; and identical to cultured borreliae following exposure to hyperimmune sera and/or antibiotics. We conclude that the H9724-reactive structures represent various forms of B. burgdorferi rather than staining artifacts. These "atypical" forms of B. burgdorferi may represent in vivo morphologic variants of this bacterium.

Acrodermatitis↗

PubMed1996

The cruciated microtubule-associated fibers of the green alga Dunaliella bioculata consist of a 31 kDa SF-assemblin.

Cytoskeletons of Dunaliella bioculata, the biflagellate wallless green alga, were isolated and analyzed using a monoclonal and a polyclonal antibody raised against SF-assemblin, the major protein of the two striated microtubule-associated fibers of the alga Spermatozopsis similis. Indirect immunofluorescence showed antigenic structures associated with the four microtubular flagellar roots. SDS-PAGE followed by immunoblot analysis revealed a cross-reacting polypeptide of 31 kDa. This protein of D. bioculata was isolated using gel filtration chromatography in 8 M urea and in vitro reassembly of striated fibers. Microsequencing of the purified protein yielded various peptides, which could be aligned along the sequence of SF-assemblin from S. similis. A complete sequence of the Dunaliella protein was obtained by cDNA cloning. It documents the non helical head domain followed by a helical rod domain with a 29 residue repeat pattern based on four heptads followed by a skip residue. Compared to SF-assemblin of S. similis the SF-assemblin of Dunaliella has a shorter head and a slightly longer rod domain. The two algal SF-assemblins share only 57% sequence identity. We conclude that SF-assemblin and related proteins in various protists are representatives of a new class of alpha-helical proteins characterized by the ability to form a special segmented coiled coil and to assemble into striated fibers of 2 nm protofilaments in vivo and in vitro.

Amino Acid Sequence↗

PubMed2006

Coarse-grained molecular dynamics simulations of a rotating bacterial flagellum.

Many types of bacteria propel themselves using elongated structures known as flagella. The bacterial flagellar filament is a relatively simple and well-studied macromolecular assembly, which assumes different helical shapes when rotated in different directions. This polymorphism enables a bacterium to switch between running and tumbling modes; however, the mechanism governing the filament polymorphism is not completely understood. Here we report a study of the bacterial flagellar filament using numerical simulations that employ a novel coarse-grained molecular dynamics method. The simulations reveal the dynamics of a half-micrometer-long flagellum segment on a timescale of tens of microseconds. Depending on the rotation direction, specific modes of filament coiling and arrangement of monomers are observed, in qualitative agreement with experimental observations of flagellar polymorphism. We find that solvent-protein interactions are likely to contribute to the polymorphic helical shapes of the filament.

Bacteria↗

PubMed2004

Effects of PNPG on cell growth cycle, motility machinery and quorum sensing in Serratia marcescens.

p-Nitrophenylglycerol (PNPG) effectively inhibits swarming of the enterobacterium Proteus mirabilis. The underlying mechanism of inhibition is unclear. We have now found that both PNPG also inhibits motility and swarming in another enterobacterium, Serratia marcescens. While the peak promoter activities of the flagellar master operon (flhDCSm), the flagellin structural gene (hagSm) and the nuclease gene (nucASm) in S. marcescens increased with increasing PNPG concentration, the expression of these genes was delayed in accordance with the reduced growth rate. As the quorum-sensing system is involved in the regulation of swarming in S. marcescens, we also examined the effect of PNPG on the production of quorum-sensing signal molecules and found that their expression was delayed with a reduced level. PNPG, therefore, had a pleiotropic effect on all aspects of S. marcescens physiology relating to swarming. The underlying molecular mechanism remains to be elucidated.

4-Butyrolactone↗

PubMedDate not supplied

[Structure and physico-chemical properties of bacterial flagella].

The structural organization of bacterial flagella was studied with Bacillus brevis and Escherichia coli MS 1350. The presence of a spherical body at the basis of a flagellum was confirmed. The structural organization of ingredients of the flagellar appratus, its inner and outer part, was investigated. The molecular weight of protein subunits in the filamentous portion of the flagellum was assayed as well as their amino acid composition. The mode of attachment of the flagellum to the cell is discussed.

Amino Acids↗

PubMed1976

Antigenic structures of Salmonella flagella. I. Presence of an antigenic determinant exposed at one end of flagellar fragments.

Salmonella flagellin, which is a constitutional subunit of the flagellum, was shown to have antigenic determinants distinct from its own serotypic ones. These antigenic determinants were found to be common to flagellins from the so-called g-complex serotypes, such as fg, mt, gm, gt, gp and gmptu, but not to those from other serotypes, such as a, i or enx. Rabbits immunized with flagellin of serotype "fg" produced anti-"fg" flagellin antibodies. Only about 20 percent of these corresponded to the serotype determinants of the "fg" on the surface of the flagella, and the remaining 80 percent reacted with the flagellin of the unrelated serotype "mt", and corresponded to the distinct determinants common to the flagellin molecules. These antigenic determinants were detected by the immunoferritin technique at only one, not both, terminals of the flagellar fragments, suggesting that a unidirectional arrangement of flagellin subunits in the flagella may expose the inherent conformation of the subunits at only one end of the flagellum.

Antibodies, Bacterial↗

PubMed1998

[The movement of the human spermatozoon].

The human sperm flagellum is composed by an axoneme made up of peripheral doublets of longitudinal microtubules on which are fixed dynein arms and radial spokes. A mechanochemical cycle of attachment-detachment of dynein arms on the adjacent microtubules results in a sliding/bending or microtubules. This process repeated along the flagellum, induces the propagation of a wave. The progressive movement of ejaculated spermatozoa is modified during their transport through the feminal genital tract under the influence of microenvironmental factors. The microfibrillar structure of cervical mucus constraints the flagellar wave amplitude whereas the tubal or follicular secretions induce an hyperactivation of the movement characterized by a loss of progression and a high degree of flagellar curvature. Sperm movement modifications are depending on external regulatory factors among which some could be secreted by the oocyte or by the perioocyte layers to create a sperm chemotaxis which would optimize the gametic interaction. The external factors modulate sperm movement through their interaction with membrane "receptors" and intracellular messengers such as cyclic AMP, ATP, Calcium, pH. These latter control dynein-microtubules interaction through a phosphorylation-dephosphorylation process of axonemal proteins.

Flagella↗

PubMed2006

Two DNA invertases contribute to flagellar phase variation in Salmonella enterica serovar Typhimurium strain LT2.

Salmonella enterica serovar Typhimurium strain LT2 possesses two nonallelic structural genes, fliC and fljB, for flagellin, the component protein of flagellar filaments. Flagellar phase variation occurs by alternative expression of these two genes. This is controlled by the inversion of a DNA segment, called the H segment, containing the fljB promoter. H inversion occurs by site-specific recombination between inverted repetitious sequences flanking the H segment. This recombination has been shown in vivo and in vitro to be mediated by a DNA invertase, Hin, whose gene is located within the H segment. However, a search of the complete genomic sequence revealed that LT2 possesses another DNA invertase gene that is located adjacent to another invertible DNA segment within a resident prophage, Fels-2. Here, we named this gene fin. We constructed hin and fin disruption mutants from LT2 and examined their phase variation abilities. The hin disruption mutant could still undergo flagellar phase variation, indicating that Hin is not the sole DNA invertase responsible for phase variation. Although the fin disruption mutant could undergo phase variation, fin hin double mutants could not. These results clearly indicate that both Hin and Fin contribute to flagellar phase variation in LT2. We further showed that a phase-stable serovar, serovar Abortusequi, which is known to possess a naturally occurring hin mutation, lacks Fels-2, which ensures the phase stability in this serovar.

Amino Acid Sequence↗

PubMed2003

Host-parasite interactions and trypanosome morphogenesis: a flagellar pocketful of goodies.

Trypanosomes are characterised by the possession of a single flagellum and a subpellicular microtubule cytoskeleton. The flagellum is more than an organelle for motility; its position and polarity along with the sub-pellicular cytoskeleton enables the morphogenesis of a distinct flagellar pocket and the flagellar basal body is responsible for positioning and segregating the kinetoplast--the mitochondrial genome. Recent work has highlighted the molecules and morphogenesis of these cytoskeletal/flagellum structures and how dynamic events, occurring in the flagellar pocket and kinetoplast, are critical for host-parasite interactions.

Animals↗

PubMed2004

Evolution and divergence of the genes for cytoplasmic, mitochondrial, and flagellar creatine kinases.

Creatine kinase (CK) plays a central role in energy homeostasis in cells that display high and variable rates of energy turnover. A number of CK genes exist, each being targeted to particular intracellular compartments. In the vertebrates, two genes code for proteins which form homo- and heterodimers targeted to the cytoplasm, while two additional genes code for primarily octameric proteins targeted to the mitochondrial intermembrane space. Yet another gene is present in certain groups which codes for three fused, complete CK domains and is typically targeted to the flagellar membrane of primitive-type spermatozoa. CK is widely distributed in protochordates and both protostome and deuterostome invertebrate groups. The evolutionary relationships of these CK genes have not been fully elucidated. The present communication reports new cDNA-derived deduced amino acid sequences for four cytoplasmic and three mitochondrial CKs and one flagellar CK from lophotrochozoan, protostome invertebrates as well as a new cytoplasmic CK sequence from a protochordate tunicate. These new sequences, coupled with available sequences in the databases and sequences extracted from genome sequencing projects, provide revealing insights into the evolution and divergence of CK genes. Phylogenetic analyses showed that single cytoplasmic, mitochondrial, and flagellar CK genes were present prior to the divergence of the protostomes and deuterostomes. The flagellar CK gene may have evolved within the cytoplasmic gene clade, although the evidence is somewhat equivocal. The two cytoplasmic genes in the vertebrates, and most likely the two mitochondrial genes, evolved after the divergence of the craniates from the protochordates. Comparison of the structure of the genes for selected cytoplasmic, mitochondrial, and flagellar CKs revealed two identical intron boundaries, further reinforcing the notion of a common evolutionary origin, but also showed patterns of changes in structure consistent with each gene type. These studies show that the cytoplasmic, mitochondrial, and flagellar CK genes are rather ancient and that there has been a systematic pattern of duplication and divergence consistent with changing nature of energy demands and physicochemical environment in the cells where they are expressed.

Amino Acid Sequence↗

PubMed1978

Interrelationships between microtubules, a striated fiber, and the gametic mating structure of Chlamydomonas reinhardi.

The microtubule system associated with the Chlamydomonas reinhardi flagellar apparatus is shown to differ from previous descriptions; two of the four flagellar "roots" possess only two microtubules and are associated with a finely striated fiber. In gametic cells this fiber underlies the gametic mating structure and makes contact with it. Functional interpretations are offered.

Animals↗

PubMed2025

Structural properties of short-chain carboxylic acids and alcohols relate to the molecular and physiological response of Salmonella enterica in an acidic environment.

Short-chain carboxylic acids (SCCA) and short-chain alcohols (SCALC) are naturally occurring antimicrobials that contribute to the biopreservation of food fermentations. This study investigated the effect of structurally different SCCA/SCALC with two-carbon (acetic acid; phenylacetic acid; 2-phenylethanol), three-carbon (propionic acid; 3-phenylpropionic acid; 3-phenylpropanol), and three-carbon chain with an additional hydroxyl group (lactic acid; 3-phenyllactic acid; 1-phenylpropanol) on the fitness, metabolic activity and gene expression of the pathogen Salmonella enterica at pH 4.5. SCCA inhibited Salmonella at lower concentrations than SCALC with the exception of lactic acid, which was partly consumed. The presence of a phenyl group enhanced antimicrobial activity. SCCA but not SCALC increased the lag phase of S. enterica, and in general, acetate was formed when cell growth was reduced by 20% suggesting a negative impact on bacteria fitness. Principal component analysis and hierarchical clustering indicated distinct gene expression profiles of S. enterica in response to SCCA or SCALC. In the presence of certain SCCA/SCALC, Salmonella activated pathways related to cellular pH control, and 1,2-propanediol, propionic acid and ethanolamine metabolism that involved the formation of metabolosomes. Genes related to flagellar assembly were less expressed and mobility was lower in the presence of lactic and 3-phenyllactic acid compared to controls suggesting a compound-specific response. KEY POINTS: • Differences in response among structurally different SCCA/SCALC at acidic condition. • SCCA/SCALC stress interfered with cell growth and metabolism of acetic and propionic acid. • Lactic acid prolonged the lag phase and reduced motility of Salmonella.

Salmonella enterica↗

PubMed2004

Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella.

FlhA is an integral membrane component of the Salmonella type III flagellar protein export apparatus. It consists of 692 amino acid residues and has two domains: the N-terminal transmembrane domain consisting of the first 327 amino acid residues, and the C-terminal cytoplasmic domain (FlhAC) comprising the remainder. Here, we have investigated the structure and function of FlhAC. DNA sequence analysis revealed that temperature-sensitive flhA mutations, which abolish flagellar protein export at the restrictive temperature, lie in FlhAC, indicating that FlhAC plays an important role in the protein export process. Limited proteolysis of purified His-FlhAC by trypsin and V8 showed that only a small part of FlhAC near its N terminus (residues 328-351) is sensitive to proteolysis. FlhAC38K, the smallest fragment produced by V8 proteolysis, is monomeric and has a spherical shape as judged by analytical gel filtration chromatography and analytical ultracentrifugation. The far-UV CD spectrum of FlhAC38K showed that it contains considerable amounts of secondary structure. FlhA(Delta328-351) missing residues 328-351 failed to complement the flhA mutant, indicating that the proteolytically sensitive region of FlhA is important for its function. FlhA(Delta328-351) was inserted into the cytoplasmic membrane, and exerted a strong dominant negative effect on wild-type cells, suggesting that it retains the ability to interact with other export components within the cytoplasmic membrane. Overproduced FlhAC38K inhibited both motility and flagellar protein export of wild-type cells to some degree, suggesting that FlhAC38K is directly involved in the translocation reaction. Amino acid residues 328-351 of FlhA appear to be a relatively flexible linker between the transmembrane domain and FlhAC38K.

Amino Acid Sequence↗

PubMed2001

Molecular characterization of fliD gene encoding flagellar cap and its expression among Clostridium difficile isolates from different serogroups.

The fliD gene encoding the flagellar cap protein (FliD) of Clostridium difficile was studied in 46 isolates belonging to serogroups A, B, C, D, F, G, H, I, K, X, and S3, including 30 flagellated strains and 16 nonflagellated strains. In all but three isolates, amplification by PCR and reverse transcription-PCR demonstrated that the fliD gene is present and transcribed in both flagellated and nonflagellated strains. PCR-restriction fragment length polymorphism (RFLP) analysis of amplified fliD gene products revealed interstrain homogeneity, with one of two major patterns (a and b) found in all but one of the strains, which had pattern c. A polyclonal monospecific antiserum raised to the recombinant FliD protein reacted in immunoblots with crude flagellar preparations from 28 of 30 flagellated strains but did not recognize FliD from nonflagellated strains. The fliD genes from five strains representative of the three different RFLP groups were sequenced, and sequencing revealed 100% identity between the strains with the same pattern and 88% identity among strains with different patterns. Our results show that even though FliD is a structure exposed to the outer environment, the flagellar cap protein is very well conserved, and this high degree of conservation suggests that it has a very specific function in attachment to cell or mucus receptors.

Bacterial Proteins↗

PubMed1997

A model for flagellar motility.

Experimental investigation has provided a wealth of structural, biochemical, and physiological information regarding the motile mechanism of eukaryotic flagella/cilia. This chapter surveys the available literature, selectively focusing on three major objectives. First, it attempts to identify those conserved structural components essential to providing motile function in eukaryotic axonemes. Second, it examines the relationship between these structural elements to determine the interactions that are vital to the mechanism of flagellar/ciliary beating. Third, the vital principles of these interactions are incorporated into a tractable theoretical model, referred to as the Geometric Clutch, and this hypothetical scheme is examined to assess its compatibility with experimental observations.

Animals↗

PubMed2006

The sperm of Hylodinae species (Anura, Leptodactylidae): ultrastructural characteristics and their relevance to interspecific taxonomic relationships.

Hylodinae leptodactylids (sensu Lynch 1971) form a group of diurnal frogs, which is hypothesized on the basis of morphological traits to be the closest relatives of the dendrobatid frogs. Our study describes ultrastructural characteristics of sperm from three hylodine species (Hylodes phyllodes, Crossodactylus sp. n. and Megaelosia massarti) to reassess the intergeneric relationships within the Hylodinae, as well as the supposed relationship between the Hylodinae and Dendrobatidae. The ultrastructure of the sperm is very similar among the three species and is indicative of its conserved nature within the Hylodinae. The structure of the acrosomal complex was very similar to that of other leptodactylid species, to most of the remaining species included in the Bufonoidea lineage, and also to that observed in the dendrobatid species examined so far. Since such a structure has been considered a plesiomorphic trait, it contributes little to our understanding of the relationships between the Hylodinae and Dendrobatidae. The flagellar apparatus of Crossodactylus sp. n. is very similar to that of most leptodactylids. The sperm of Megaelosia massarti and Hylodes phyllodes display a distinctive condition in their axial and juxtaxonemal fibers. This distinctive flagellar condition expands the already known variability in sperm structure within the Leptodactylidae.

Acrosome↗