The Intracellular Localization of Pseudomonas aeruginosa Lectins

Glick, Jane M.; Garber, N.

doi:10.1099/00221287-129-10-3085

Cited by 43 publications

(45 citation statements)

References 24 publications

(18 reference statements)

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“…These observations, combined with the properties of lectins, led us to hypothesize that the lectins in P. aeruginosa may exert some effect on surface-exposed proteins. Although both P. aeruginosa lectins were initially thought to be located in the cytoplasm (11), later results suggested that LecB may be present on the surface of sessile Pseudomonas cells (20).…”

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confidence: 99%

Pseudomonas aeruginosa LecB Is Involved in Pilus Biogenesis and Protease IV Activity but Not in Adhesion to Respiratory Mucins

2006

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Pseudomonas aeruginosa expresses two lectins which are implicated in adhesion and biofilm formation. In this study, we demonstrate that P. aeruginosa LecB is involved in pilus biogenesis and proteolytic activity. Moreover, neither lectin was involved in adhesion to human tracheobronchial mucin. We infer that some of the ascribed functions are secondary effects on other systems rather than effects of the lectins themselves.

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confidence: 99%

Pseudomonas aeruginosa LecB Is Involved in Pilus Biogenesis and Protease IV Activity but Not in Adhesion to Respiratory Mucins

2006

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“…Recent observations suggest that GSLs might be of critical importance for the internalization of P. aeruginosa into nonphagocytic cells (9). The homotetrameric, galactophilic lectin LecA, which is localized to the outer bacterial membrane (21), belongs to the carbohydrate binding proteins expressed by P. aeruginosa that recognize GSLs (22,23) and represents one of the virulence factors (24). The preferential binding of LecA to the GSL globotriaosylceramide (also known as Gb3/CD77 or Pk histo-blood group antigen) (22,25) prompted us to investigate the role of LecA-Gb3 interaction in the cellular uptake of P. aeruginosa.…”

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confidence: 99%

A lipid zipper triggers bacterial invasion

Eierhoff

Bastian

Thuenauer

et al. 2014

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

127

161

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Significance Entry of bacteria into host cells critically depends on their proper engulfment by the plasma membrane. So far, actin polymerization has been described as a major driving force in this process. However, our study reveals that the interaction of the bacterial surface lectin LecA with the host cell glycosphingolipid Gb3 is fully sufficient to promote engulfment of Pseudomonas aeruginosa , whereas actin polymerization is dispensable. Hence, the formation of a “lipid zipper” represents a previously unidentified mechanism of bacterial uptake and demonstrates that bacterial pathogens have evolved lipid-based invasion strategies that may function in addition to protein receptor-based ones. Furthermore, by identifying the LecA/Gb3 interaction as the major invasion-promoting factor, our study provides new targets for drugs that may prevent bacterial invasion and dissemination.

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“…Different subcellular localization sites have been suggested for the mannose-/fucose-specific lectin LecB during recent years. A significant portion of the lectin has been found to reside in the cytoplasm (14), and in addition to the cytoplasmic localization of LecB, it has been shown that it is localized in the outer membrane of P. aeruginosa, most probably on the cell surface (50). Although this surface localization would perfectly explain the influence of LecB on biofilm formation (50), it is in fact not known at present how the protein traverses the cell envelope, since all secretion signals known in P. aeruginosa are missing (30,50).…”

Section: Resultsmentioning

confidence: 99%

“…Interestingly, LecA and LecB inhibit ciliary beating (31), hence inhibiting an important defense mechanism of the lung (2, 3). The subcellular localization of LecB has been an issue of discussion during recent years (14,50). A LecB-deficient P. aeruginosa strain was impaired in biofilm formation, and LecB was shown to be located in the outer membrane, binding to yet-unidentified ligands on the surface of biofilm cells (50).…”

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Glycosylation Is Required for Outer Membrane Localization of the Lectin LecB inPseudomonas aeruginosa

Bartels¹,

Funken

Knapp

et al. 2011

J Bacteriol

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The fucose-/mannose-specific lectin LecB from Pseudomonas aeruginosa is transported to the outer membrane; however, the mechanism used is not known so far. Here, we report that LecB is present in the periplasm of P. aeruginosa in two variants of different sizes. Both were functional and could be purified by their affinity to mannose. The difference in size was shown by a specific enzyme assay to be a result of N glycosylation, and inactivation of the glycosylation sites was shown by site-directed mutagenesis. Furthermore, we demonstrate that this glycosylation is required for the transport of LecB.Lectins are proteins of nonimmune origin that recognize and bind to specific carbohydrate structural epitopes without modifying them. This group of carbohydrate proteins function as central mediators of information transfer in biological systems and perform their duties by interacting with glycoproteins, glycolipids, and oligosaccharides (34). Lectins exist in a wide range of organisms, including viruses, bacteria, plants, and animals, and are believed to play a general and important role in cell-cell interactions (9). Many bacteria have an arsenal of different lectins for targeting glycosylated proteins of the host (21). One example, the lectin FimH at the top of type 1 pili from the uropathogenic Escherichia coli, recognizes terminally located D-mannose moieties on cell-bound glycoproteins to mediate adhesion between the bacterium and the urothelium (4, 20). Lectins are also of interest for medical and pharmaceutical applications, as exemplified by the galactoside-specific mistletoe lectin, which is widely used as a drug to support anticancer therapy (5).Pseudomonas aeruginosa, an opportunistic pathogen associated with chronic airway infections, synthesizes two lectins, LecA and LecB (formerly also named PA-IL and PA-IIL) (11). Strains of P. aeruginosa which produce high levels of these virulence factors exhibit an increased virulence potential (12). Both lectins play a prominent role in human infection, since it was demonstrated that P. aeruginosa-induced otitis externa diffusa (46), as well as P. aeruginosa in respiratory tract infections (56) and cystic fibrosis patients (16), could successfully be treated by the application of a solution containing specific sugars. The sugar solutions presumably prevented lectin-mediated bacterial adhesion to the corresponding host cells. The expression of lectin genes in P. aeruginosa is coordinately regulated with certain other virulence factors and controlled via the quorum-sensing cascade and by the alternative sigma fac-

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The Intracellular Localization of Pseudomonas aeruginosa Lectins

Cited by 43 publications

References 24 publications

Pseudomonas aeruginosa LecB Is Involved in Pilus Biogenesis and Protease IV Activity but Not in Adhesion to Respiratory Mucins

Pseudomonas aeruginosa LecB Is Involved in Pilus Biogenesis and Protease IV Activity but Not in Adhesion to Respiratory Mucins

A lipid zipper triggers bacterial invasion

Glycosylation Is Required for Outer Membrane Localization of the Lectin LecB inPseudomonas aeruginosa

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