Role of LecA and LecB Lectins in
            <i>Pseudomonas aeruginosa</i>
            -Induced Lung Injury and Effect of Carbohydrate Ligands

Chemani, Chanez; Imberty, Anne; Bentzmann, Sophie de; Martineau, Pierre; Wimmerová, Michaela; Guery, Benoît; Faure, Karine

doi:10.1128/iai.01204-08

Cited by 277 publications

(318 citation statements)

References 35 publications

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“…So far, LecA has been related to bacterial adhesion and biofilm formation (20,48) and represents one of the virulence factors contributing to lung injury during infection (24). Our data identify LecA as an invasion factor for P. aeruginosa, which might contribute to the dissemination of the pathogen within its host organism during infection.…”

Section: Discussionmentioning

confidence: 82%

“…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%

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A lipid zipper triggers bacterial invasion

Eierhoff

Bastian

Thuenauer

et al. 2014

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

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128

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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Section: Discussionmentioning

confidence: 82%

mentioning

confidence: 99%

A lipid zipper triggers bacterial invasion

Eierhoff

Bastian

Thuenauer

et al. 2014

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

Self Cite

128

161

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“…A variety of synthetic glycoclusters 8 have been investigated for inhibiting LecA, 9 LecB, 10 or both, 11 and in selected cases for their effects in controlling P. aeruginosa infections in vivo. 12 This review focuses on a related effort to develop inhibitors of LecA and LecB on the basis of glycopeptide dendrimers.…”

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confidence: 99%

Glycopeptide dendrimers as Pseudomonas aeruginosa biofilm inhibitors

2013

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Synthetic glycopeptide dendrimers composed of a branched oligopeptide tree structure appended with glycosidic groups at its multiple N-termini were investigated for binding to the Pseudomonas aeruginosa lectins LecB and LecA. These lectins are partly responsible for the formation of antibiotic resistant biofilms in the human pathogenic bacterium P. aeruginosa, which causes lethal airway infections in immune-compromised and cystic fibrosis patients. Glycopeptide dendrimers with high affinity to the lectins were identified by screening of combinatorial libraries. Several of these dendrimers, in particular the LecB specific glycopeptide dendrimers FD2 and D-FD2 and the LecA specific glycopeptide dendrimers GalAG2 and GalBG2, also efficiently block P. aeruginosa biofilm formation and induce biofilm dispersal in vitro. Structure-activity relationship and structural studies are reviewed, in particular the observation that multivalency is essential to the anti-biofilm effect in these dendrimers.

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“…This is significant as invasion of lung epithelial cells by Bcc depends on asialylated glycolipids [13]. In addition, alterations in specific fucosyl residues of membrane glycopeptides of CF cells provide receptors for a fucose-specific P. aeruginosa lectin that is involved in P. aeruginosa pathogenicity [14]. Furthermore, increased glycosaminoglycan levels have been observed in CF airways as recently reviewed by Reeves et al [15] and may contribute to CF lung disease.…”

Section: Role Of Cftr In Cf Lung Colonisationmentioning

confidence: 98%

Bacterial host interactions in cystic fibrosis

Callaghan

McClean

2012

Current Opinion in Microbiology

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This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues.Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited.In most cases authors are permitted to post their version of the article (e.g. in Word or Tex form) to their personal website or institutional repository. Authors requiring further information regarding Elsevier's archiving and manuscript policies are encouraged to visit:http://www.elsevier.com/copyrightAuthor's personal copy Bacterial host interactions in cystic fibrosis Má ire Callaghan and Siobhá n McCleanChronic infection is a hallmark of cystic fibrosis (CF) and the main contributor to morbidity. Microbial infection in CF is complex, due to the number of different species that colonise the CF lung. Their colonisation is facilitated by a host response that is impaired or compromised by highly viscous mucous, zones of hypoxia and the lack of the cystic fibrosis transmembrane regulator (CFTR). Successful dominant CF pathogens combine an effective arsenal to establish infection and counter-attack the host response, together with an ability to adapt readily to an unfavourable environment. Hypermutability is common among CF pathogens facilitating adaptation and as the host response persists, progressive destruction of the normal architecture of lung tissue ensues with catastrophic consequences for the host. Limited information exists on the host-microbial interactions of many of these organisms and this review will focus only on the current understanding of the more clearly defined CF pathogens (Box 1). Role of CFTR in CF lung colonisationA direct role of the CFTR mutation in CF pathogenesis has been attributed to normal CFTR acting as a pathogen receptor involved in the internalisation and subsequent clearance of P. aeruginosa [9], but this mechanism is pathogen-specific. Mutated CFTR has also been attributed to be the cause of reduced internalisation of one Bcc species, Burkholderia dolosa, but not the more virulent Burkholderia cenocepacia in respiratory epithelial cells [10]. Furthermore, in contrast to P. aeruginosa, S. aureus was more invasive of CF cells compared to non-CF cells [11], indicating that CFTR is not the only route of bacterial uptake and invasion into the epithelium.Alterations in the phenotype of CF airway epithelial cells also provide receptors for pathogens to adhere to. For example, CF airways show alterations in membrane glycoproteins and glycolipids which are directly linked to the CFTR defect (reviewed by [12]). The ratio of asialylated to sialylated glycolipids is higher in CF cells compared to non-CF cells, providing additional receptors for P. aeruginosa and Bcc. This is significant as invasion of lung epithelial cells by Bcc depends on asialylated glycolipids [13]. In addition, alteration...

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Role of LecA and LecB Lectins in Pseudomonas aeruginosa -Induced Lung Injury and Effect of Carbohydrate Ligands

Cited by 277 publications

References 35 publications

A lipid zipper triggers bacterial invasion

A lipid zipper triggers bacterial invasion

Glycopeptide dendrimers as Pseudomonas aeruginosa biofilm inhibitors

Bacterial host interactions in cystic fibrosis

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