Pili in Gram-positive pathogens

Telford, John L.; Barocchi, Michèle A.; Margarit, Immaculada; Rappuoli, Rino; Grandi, Guido

doi:10.1038/nrmicro1443

Cited by 395 publications

(438 citation statements)

References 61 publications

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“…We attributed this hyperthinness to the covalent cross-linkage between the monomers. The sum of noncovalent interactions in such a small cross-section alone would not be sufficient to allow stable axial elongation of the fibril, which may be one of the reasons that the native pili of gram-positive bacteria also rely on covalent cross-linkages between subunits but in a different form than in our system [25][26][27] .…”

Section: Discussionmentioning

confidence: 93%

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Hyperthin nanochains composed of self-polymerizing protein shackles

et al. 2013

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Protein fibrils are expected to have applications as functional nanomaterials because of their sophisticated structures; however, nanoscale ordering of the functional units of protein fibrils remains challenging. Here we design a series of self-polymerizing protein monomers, referred to as protein shackles, derived from modified recombinant subunits of pili from Streptococcus pyogenes. The monomers polymerize into nanochains through spontaneous irreversible covalent bond formation. We design the protein shackles so that their reactions can be controlled by altering redox conditions, which affect disulphide bond formation between engineered cysteine residues. The interaction between the monomers improves their polymerization reactivity and determines morphologies of the polymers. In addition, green fluorescent protein-tagged protein shackles can polymerize, indicating proteins can be stably attached to the nanochains with its functionality preserved. Furthermore we demonstrate that a molecular-recognizable nanochain binds to its partner with an enhanced binding ability in solution. These characteristics are expected to be applied for novel protein nanomaterials.

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Section: Discussionmentioning

confidence: 93%

“…Pili, long filamentous protein structures that extend from bacterial surfaces 24 , form by covalent polymerization of subunits catalysed by an enzyme called sortase [25][26][27] . As pilus subunits are arranged head-to-tail, pili are thin (2-5 nm).…”

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confidence: 99%

Hyperthin nanochains composed of self-polymerizing protein shackles

et al. 2013

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“…Cell adhesion molecules also have key roles in mediating cellular processes such as cell-cell communication (Dalva et al, 2007), tissue development (Morgan et al, 2007), inflammation (Weber et al, 2007), cancer (Gray-Owen and Blumberg, 2006) and microbial infection (Verstrepen et al, 2004;Kolter and Greenberg, 2006;Telford et al, 2006;Sokurenko et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Atomic force microscopy – looking at mechanosensors on the cell surface

Heinisch

Lipke

Beaussart

et al. 2012

Journal of Cell Science

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SummaryLiving cells use cell surface proteins, such as mechanosensors, to constantly sense and respond to their environment. However, the way in which these proteins respond to mechanical stimuli and assemble into large complexes remains poorly understood at the molecular level. In the past years, atomic force microscopy (AFM) has revolutionized the way in which biologists analyze cell surface proteins to molecular resolution. In this Commentary, we discuss how the powerful set of advanced AFM techniques (e.g. live-cell imaging and single-molecule manipulation) can be integrated with the modern tools of molecular genetics (i.e. protein design) to study the localization and molecular elasticity of individual mechanosensors on the surface of living cells. Although we emphasize recent studies on cell surface proteins from yeasts, the techniques described are applicable to surface proteins from virtually all organisms, from bacteria to human cells.

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“…However, unlike Gramnegative pili, which, due to the structural elasticity of their subunit constituents, would be able to retract reversibly and pull microbes closer to the host cells (17,20,26), pili from Gram-positive bacteria appear to consist of inextensible pilin subunits (2), making them more rigid and less apt to function in a similar manner. Consequently, the SpaCBA pilus-mediated binding in L. rhamnosus GG that brings LPXTG-like surface adhesins (e.g., MBF and MabA) closer to the mucus layer could expectedly be less dynamic and more arbitrary, possibly relying on the "zipper-like" mechanistic explanation of adhesion in piliated Gram-positive pathogens described previously (38). On the other hand, collectively, such a multiplicity of adhesive interactions, including those of MBF, will undoubtedly allow L. rhamnosus GG to be better embedded in the intestinal mucosa for what can be regarded as its increased capacity of persistence in the intestine.…”

Section: Vol 77 2011 Mucus-specific Surface Adhesin From L Rhamnosmentioning

confidence: 99%

Functional Characterization of a Mucus-Specific LPXTG Surface Adhesin from Probiotic Lactobacillus rhamnosus GG

Ossowski

Satokari

Reunanen

et al. 2011

Appl Environ Microbiol

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In spite of the wealth of clinical evidence supporting the health benefits of Lactobacillus rhamnosus GG in humans, there is still a lack of understanding of the molecular mechanisms behind its probiosis. Current knowledge suggests that the health-promoting effects of this probiotic strain might be partly dependent on its persistence in the intestine and adhesion to mucosal surfaces. Moreover, L. rhamnosus GG contains mucusbinding pili that might also explain the occupation of its ecological niche as a comparatively less stringent allochthonous intestine-dwelling bacterium. To uncover additional surface proteins involved in mucosal adhesion, we investigated the adherence properties of the only predicted protein (LGG_02337) in L. rhamnosus GG that exhibits homology with a known mucus-binding domain. We cloned a recombinant form of the gene for this putative mucus adhesin and established that the purified protein readily adheres to human intestinal mucus. We also showed that this mucus adhesin is visibly distributed throughout the cell surface and participates in the adhesive interaction between L. rhamnosus GG and mucus, although less prominently than the mucus-binding pili in this strain. Based on primary structural comparisons, we concluded that the current annotation of the LGG_02337 protein likely does not accurately reflect its predicted properties, and we propose that this mucus-specific adhesin be called the mucus-binding factor (MBF). Finally, we interpret our results to mean that L. rhamnosus GG MBF, as an active mucus-specific surface adhesin with a presumed ancillary involvement in pilus-mediated mucosal adhesion, plays a part in the adherent mechanisms during intestinal colonization by this probiotic.The commensal Gram-positive lactobacilli are one of the first groups of bacteria to inhabit the human gastrointestinal (GI) tract (16) and include some strains (autochthonous) that colonize the intestine stably throughout the lifetime of the host (31). In addition, there are those strains, called allochthonous, that persist only briefly in the intestine, many of these being probiotics (1, 9, 13) and understood to stimulate health-benefiting immune responses in host intestinal cells (for a review, see reference 14) or cause competitive displacement of invading pathogens (for a review, see reference 35). Thus far, the precise molecular mechanisms that differentiate the colonization ability between autochthonous and allochthonous intestinal lactobacilli remain undefined (42), although they are likely to be partly dependent on a diverse range of cell surface adhesion molecule-mediated interactions with the host intestinal mucosa. With that being said, there are a growing number of reports in the literature that indicate that lactobacillar adherence to the intestinal mucosal layer is mediated by surface proteins with a mucus-binding capacity (15,21,22,25,30,32,33,41). Moreover, homology-driven genome mining in several Lactobacillus spp. (3,7,8,11,33) has identified the presence of various-sized putative mucus ...

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Pili in Gram-positive pathogens

Cited by 395 publications

References 61 publications

Hyperthin nanochains composed of self-polymerizing protein shackles

Hyperthin nanochains composed of self-polymerizing protein shackles

Atomic force microscopy – looking at mechanosensors on the cell surface

Functional Characterization of a Mucus-Specific LPXTG Surface Adhesin from Probiotic Lactobacillus rhamnosus GG

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