Specific Association of Lectin LecB with the Surface of Pseudomonas aeruginosa: Role of Outer Membrane Protein OprF

Funken, Horst; Bartels, Kai-Malte; Wilhelm, Susanne; Brocker, Melanie; Bott, Michael; Bains, Manjeet; Hancock, Robert E. W.; Rosenau, Frank; Jaeger, Karl‐Erich

doi:10.1371/journal.pone.0046857

Cited by 42 publications

(48 citation statements)

References 61 publications

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“…Specific LecB-OprF interaction was further demonstrated with co-purification of OprF and LecB. In the same study, a far-western blot analysis using purified LecB detected several positive protein bands from the membrane fraction of P. aeruginosa (89), suggesting that LecB may interact with other ligands on the membrane in addition to OprF. The mechanism of LecB-OprF interaction remains to be determined.…”

Section: Leca and Lecb Lectinsmentioning

confidence: 76%

“…In a study designed to identify the cell surface ligand for LecB, direct interaction between LecB and the outer membrane protein OprF was demonstrated (89). Western blot analysis revealed that OprF was necessary for proper LecB localization, as LecB was released into the culture supernatant of the oprF mutant, instead of being retained on the outer membrane as observed in the wild-type strain.…”

Section: Leca and Lecb Lectinsmentioning

confidence: 99%

“…The OMP OprF was identified in both the biofilm matrix and the OMVs (20). Since OprF interacts with the lectin LecB (89), it is possible that OMVs may be localized in the biofilm matrix via interaction of OMV-associated OprF and the potentially Psl exopolysaccharide-binding LecB, thus forming an OMV-OprF-LecB-Psl interaction. It has been documented that eDNA, a biofilm matrix component of P. aeruginosa PAO1, associates with OMVs in P. aeruginosa PAO1 (58, 109, 110), which suggests that OMVs may be involved in the process of biofilm formation by interacting with different biofilm matrix components, including eDNA.…”

Section: Outer Membrane Vesicles (Omvs)mentioning

confidence: 99%

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Biofilm Matrix Proteins

2015

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Proteinaceous components of the biofilm matrix include secreted extracellular proteins, cell surface adhesins and protein subunits of cell appendages such as flagella and pili. Biofilm matrix proteins play diverse roles in biofilm formation and dissolution. They are involved in attaching cells to surfaces, stabilizing the biofilm matrix via interactions with exopolysaccharide and nucleic acid components, developing three-dimensional biofilm architectures, and dissolving biofilm matrix via enzymatic degradation of polysaccharides, proteins, and nucleic acids. In this chapter, we will review functions of matrix proteins in a selected set of microorganisms, studies of the matrix proteomes of Vibrio cholerae and Pseudomonas aeruginosa, and roles of outer membrane vesicles and of nucleoid-binding proteins in biofilm formation.

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Section: Leca and Lecb Lectinsmentioning

confidence: 76%

Section: Leca and Lecb Lectinsmentioning

confidence: 99%

Section: Outer Membrane Vesicles (Omvs)mentioning

confidence: 99%

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Biofilm Matrix Proteins

2015

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“…The translocation of the outer membrane-associated mannose/fucose-specific lectin LecB of P. aeruginosa , that also lacks such signal sequence [50], is dependent on its glycosylation [51]. Contrary to LlpA that is exported to the culture supernatant to exert its antagonistic activity, LecB remains associated with the cell envelope through interaction with the major outer membrane protein OprF [52], in line with its role in biofilm formation.…”

Section: Discussionmentioning

confidence: 99%

Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA

et al. 2013

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Lectin-like bacteriotoxic proteins, identified in several plant-associated bacteria, are able to selectively kill closely related species, including several phytopathogens, such as Pseudomonas syringae and Xanthomonas species, but so far their mode of action remains unrevealed. The crystal structure of LlpABW, the prototype lectin-like bacteriocin from Pseudomonas putida, reveals an architecture of two monocot mannose-binding lectin (MMBL) domains and a C-terminal β-hairpin extension. The C-terminal MMBL domain (C-domain) adopts a fold very similar to MMBL domains from plant lectins and contains a binding site for mannose and oligomannosides. Mutational analysis indicates that an intact sugar-binding pocket in this domain is crucial for bactericidal activity. The N-terminal MMBL domain (N-domain) adopts the same fold but is structurally more divergent and lacks a functional mannose-binding site. Differential activity of engineered N/C-domain chimers derived from two LlpA homologues with different killing spectra, disclosed that the N-domain determines target specificity. Apparently this bacteriocin is assembled from two structurally similar domains that evolved separately towards dedicated functions in target recognition and bacteriotoxicity.

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“…Proteinaceous adhesins in the matrix have also been shown to be of utmost importance for the overall structure of the biofilm. For example, the role of lectins in the structure and robustness of the biofilm has been studied in several bacterial species, including Burkholderia cenocepacia (Inhülsen et al 2012), P. aeruginosa (Funken et al 2012) and the plantgrowth-promoting bacterium Azospirilium brasilense (Danhorn and Fuqua 2007). Lectins are sugar-binding proteins with a very specific recognition function that may bind to the EPS molecules of the matrix.…”

Section: Living Inside the Matrix: Adhesive Components Of Biofilmsmentioning

confidence: 99%

Multicellularity in Bacteria: From Division of Labor to Biofilm Formation

Aguilar

Eichwald

Eberl

2015

Evolutionary Transitions to Multicellular Life

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Introduced nearly two decades ago, the concept of multicellularity in bacteria is currently accepted as a general trait of bacterial physiology. The view of bacteria being more than just unicellular, non-organized, selfish organisms is to a large degree based on the findings that division of labor and cell-to-cell communication within bacterial communities are ubiquitous across bacterial species. Bacteria are able to form complex communities in which cells can specialize in a spatiotemporal fashion, using extracellular signals to coordinate the expression of specific genes required for structural development. Despite the enormous progress made by researchers in the field over the past years, knowledge of the molecular mechanisms that govern bacterial multicellularity and biofilm development is scarce and remains a highly interesting field for future research.

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Specific Association of Lectin LecB with the Surface of Pseudomonas aeruginosa: Role of Outer Membrane Protein OprF

Cited by 42 publications

References 61 publications

Biofilm Matrix Proteins

Biofilm Matrix Proteins

Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA

Multicellularity in Bacteria: From Division of Labor to Biofilm Formation

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