Adhesion to cellulose of the Gram-positive bacterium Ruminococcus albus involves type IV pili
               The EMBL accession number for the sequence reported in this paper is AJ416469.

Rakotoarivonina, Harivony; Jubelin, Grégory; Hébraud, Michel; Gaillard-Martinie, Brigitte; Forano, Evelyne; Mosoni, Pascale

doi:10.1099/00221287-148-6-1871

Cited by 79 publications

(69 citation statements)

References 40 publications

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“…Western immunoblots showed there were no differences among the wild-type and mutants strains examined with respect to CbpC production, but the adhesion-defective mutants of R. albus strain 20 are known to be defective in production of this protein (34,42). These differences among mutant strains further support the contention that R. albus employs multiple strategies for adhesion to cellulose, including one that is coordinated via type 4 fimbrial structures and another that is more intimately associated with the cellulolytic apparatus of the bacterium.…”

Section: Vol 186 2004 R Albus Mutants Defective In Cellulose Degramentioning

confidence: 99%

“…What sets R. albus further apart from the other cellulolytic bacteria is that its ability to grow effectively with cellulose is conditional on the availability of phenylacetic acid (PAA) and phenylpropionic acid (PPA) and that adhesion to cellulose appears to be mediated, at least in part, by the formation of type 4 fimbria-like structures (34,38,42). Measurable quantities of both PAA and PPA are present in ruminal fluid, and only micromolar amounts of these compounds elicit substantial changes in cell surface ultrastructure and cellulase activity (47,48).…”

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Ruminococcus albus 8 Mutants Defective in Cellulose Degradation Are Deficient in Two Processive Endocellulases, Cel48A and Cel9B, Both of Which Possess a Novel Modular Architecture

et al. 2004

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The cellulolytic bacterium Ruminococcus albus 8 adheres tightly to cellulose, but the molecular biology underpinning this process is not well characterized. Subtractive enrichment procedures were used to isolate mutants of R. albus 8 that are defective in adhesion to cellulose. Adhesion of the mutant strains was reduced 50% compared to that observed with the wild-type strain, and cellulose solubilization was also shown to be slower in these mutant strains, suggesting that bacterial adhesion and cellulose solubilization are inextricably linked. Two-dimensional polyacrylamide gel electrophoresis showed that all three mutants studied were impaired in the production of two high-molecular-mass, cell-bound polypeptides when they were cultured with either cellobiose or cellulose. The identities of these proteins were determined by a combination of mass spectrometry methods and genome sequence data for R. albus 8. One of the polypeptides is a family 9 glycoside hydrolase (Cel9B), and the other is a family 48 glycoside hydrolase (Cel48A). Both Cel9B and Cel48A possess a modular architecture, Cel9B possesses features characteristic of the B 2 (or theme D) group of family 9 glycoside hydrolases, and Cel48A is structurally similar to the processive endocellulases CelF and CelS from Clostridium cellulolyticum and Clostridium thermocellum, respectively. Both Cel9B and Cel48A could be recovered by cellulose affinity procedures, but neither Cel9B nor Cel48A contains a dockerin, suggesting that these polypeptides are retained on the bacterial cell surface, and recovery by cellulose affinity procedures did not involve a clostridium-like cellulosome complex. Instead, both proteins possess a single copy of a novel X module with an unknown function at the C terminus. Such X modules are also present in several other R. albus glycoside hydrolases and are phylogentically distinct from the fibronectin III-like and X modules identified so far in other cellulolytic bacteria.

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Section: Vol 186 2004 R Albus Mutants Defective In Cellulose Degramentioning

confidence: 99%

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confidence: 99%

Ruminococcus albus 8 Mutants Defective in Cellulose Degradation Are Deficient in Two Processive Endocellulases, Cel48A and Cel9B, Both of Which Possess a Novel Modular Architecture

et al. 2004

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“…Another attachment mode by means of pili has been described for several gram-negative pathogenic bacteria, including, for example, Neisseria meningitidis, N. gonorrhoeae (22,36), and Pseudomonas aeruginosa (38), and for some grampositive bacteria, such as Enterococcus faecalis (11), Actinomyces spp. (19), and Ruminococcus albus (28). So far there is no experimental evidence that members of the genus Deinococcus produce flagella or pili, even though several genes encoding pilus-associated functions have been found in the genome of D. radiodurans (20).…”

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Characterization of Adhesion Threads of Deinococcus geothermalis as Type IV Pili

et al. 2006

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Deinococcus geothermalis E50051 forms tenuous biofilms on paper machine surfaces. Field emission electron microscopy analysis revealed peritrichous appendages which mediated cell-to-surface and cell-to-cell interactions but were absent in planktonically grown cells. The major protein component of the extracellular extract of D. geothermalis had an N-terminal sequence similar to the fimbrial protein pilin annotated in the D. geothermalis DSM 11300 draft sequence. It also showed similarity to the type IV pilin sequence of D. radiodurans and several gram-negative pathogenic bacteria. Other proteins in the extract had N-terminal sequences identical to D. geothermalis proteins with conservative motifs for serine proteases, metallophosphoesterases, and proteins whose function is unknown. Periodic acid-Schiff staining for carbohydrates indicated that these extracellular proteins may be glycosylated. A further confirmation for the presence of glycoconjugates on the cell surface was obtained by confocal laser scanning imaging of living D. geothermalis cells stained with Amaranthus caudatus lectin, which specifically binds to galactose residues. The results indicate that the thread-like appendages of D. geothermalis E50051 are glycosylated type IV pili, bacterial attachment organelles which have thus far not been described for the genus Deinococcus.Deinococcus geothermalis is an important primary biofilm former found in paper machine water (17,35). It forms tenuous biofilms on abiotic surfaces and is difficult or impossible to remove from the surfaces using industrial washing procedures (18). The attachment of D. geothermalis involves thread-like structures that connect the cells to the abiotic surface while allowing sliding movement, to escape mechanical stress (18).Capsules and slimes are involved in the adhesion of bacteria onto living and nonliving substrates (6, 15). However, adhesion of D. geothermalis seems to occur in the absence of either of these (18,29). Another attachment mode by means of pili has been described for several gram-negative pathogenic bacteria, including, for example, Neisseria meningitidis, N. gonorrhoeae (22,36), and Pseudomonas aeruginosa (38), and for some grampositive bacteria, such as Enterococcus faecalis (11), Actinomyces spp. (19), and Ruminococcus albus (28). So far there is no experimental evidence that members of the genus Deinococcus produce flagella or pili, even though several genes encoding pilus-associated functions have been found in the genome of D. radiodurans (20). Within the phylum Deinococcus-Thermus, only the Thermus thermophilus strain HB27 has been reported to express pili during natural transformation (8).This study describes the ultrastructure of the thread-like appendages expressed by the industrially relevant strain D. geothermalis E50051. It is proposed that they represent pili and glycoconjugates necessary for adhesion and biofilm formation of D. geothermalis. MATERIALS AND METHODSBacterial strain and growth conditions. Deinococcus geothermalis E50051 (HAMBI 2411) ...

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“…adhesion ͉ aggregation ͉ pilus retraction ͉ protein crystallography T ype IV pili (Tfp) are hair-like bacterial surface filaments that have been detected in dozens of Gram-negative and Grampositive species (1)(2)(3). These organelles mediate bacterial adhesion to surfaces as diverse as stainless steel (4) and host cells (1), a property that is tightly linked to their ability to promote the formation of adhesive 3D microcolonies by mediating interbacterial interactions (5,6).…”

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3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili

Hélaine

Dyer

Nassif

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

108

144

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Type IV pili (Tfp) are widespread filamentous bacterial organelles that mediate multiple virulence-related phenotypes. They are composed mainly of pilin subunits, which are processed before filament assembly by dedicated prepilin peptidases. Other proteins processed by these peptidases, whose molecular nature and mode of action remain enigmatic, play critical roles in Tfp biology. We have performed a detailed structure/function analysis of one such protein, PilX from Neisseria meningitidis, which is crucial for formation of bacterial aggregates and adhesion to human cells. The x-ray crystal structure of PilX reveals the ␣/␤ roll fold shared by all pilins, and we show that this protein colocalizes with Tfp. These observations suggest that PilX is a minor, or low abundance, pilin that assembles within the filaments in a similar way to pilin. Deletion of a PilX distinctive structural element, which is predicted to be exposed on the filament surface, abolishes aggregation and adhesion. Our results support a model in which surface-exposed motifs in PilX subunits stabilize bacterial aggregates against the disruptive force of pilus retraction and illustrate how a minor pilus component can enhance the functional properties of pili of rather simple composition and structure.adhesion ͉ aggregation ͉ pilus retraction ͉ protein crystallography

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Adhesion to cellulose of the Gram-positive bacterium Ruminococcus albus involves type IV pili The EMBL accession number for the sequence reported in this paper is AJ416469.

Cited by 79 publications

References 40 publications

Ruminococcus albus 8 Mutants Defective in Cellulose Degradation Are Deficient in Two Processive Endocellulases, Cel48A and Cel9B, Both of Which Possess a Novel Modular Architecture

Ruminococcus albus 8 Mutants Defective in Cellulose Degradation Are Deficient in Two Processive Endocellulases, Cel48A and Cel9B, Both of Which Possess a Novel Modular Architecture

Characterization of Adhesion Threads of Deinococcus geothermalis as Type IV Pili

3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili

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