PA-I and PA-II lectin interactions with the ABO(H) and P blood group glycosphingolipid antigens may contribute to the broad spectrum adherence ofPseudomonas aeruginosa to human tissues in secondary infections

Gilboa‐Garber, Nechama; Sudakevitz, Dvora; Sheffi, Masha; Sela, Ruth; Levene, C.

doi:10.1007/bf00731276

Cited by 78 publications

(64 citation statements)

References 18 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: 70%

“…Numerous reports suggested various host cell factors, including cell surface receptors and signaling components, including α 5 β 1 integrin, cystic fibrosis transmembrane conductance regulator, and Abelson tyrosine-protein kinase 1-dependent pathway (16)(17)(18), that are involved in the cellular uptake of P. aeruginosa. Host-cell GSLs have been identified as important molecules contributing to host specificity and adhesion of P. aeruginosa (19,20). Recent observations suggest that GSLs might be of critical importance for the internalization of P. aeruginosa into nonphagocytic cells (9).…”

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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.

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: 70%

mentioning

confidence: 99%

A lipid zipper triggers bacterial invasion

Eierhoff

Bastian

Thuenauer

et al. 2014

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

128

161

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“…PA-IIL is approximately 12 to 13 kDa (24) and exhibits a high specificity for fucose (19,22,26). PA-IL and PA-IIL in addition to mannose affinity have both been shown to interact with the ABO(H) and P blood group glycosphingolipid antigens which may contribute to the tissue infectivity and pathogenicity of P. aeruginosa (27). However, in contrast to many Pseudomonas virulence determinants, there is little information concerning lectin expression at the molecular level.…”

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confidence: 99%

The Pseudomonas aeruginosa Lectins PA-IL and PA-IIL Are Controlled by Quorum Sensing and by RpoS

Falconer²,

et al. 2000

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In Pseudomonas aeruginosa, many exoproduct virulence determinants are regulated via a hierarchical quorum-sensing cascade involving the transcriptional regulators LasR and RhlR and their cognate activators, N-(3-oxododecanoyl)-L-homoserine lactone (3O-C12-HSL) and N-butanoyl-L-homoserine lactone (C4-HSL). In this paper, we demonstrate that the cytotoxic lectins PA-IL and PA-IIL are regulated via quorum sensing. Using immunoblot analysis, the production of both lectins was found to be directly dependent on the rhl locus while, in a lasR mutant, the onset of lectin synthesis was delayed but not abolished. The PA-IL structural gene, lecA, was cloned and sequenced. Transcript analysis indicated a monocistronic organization with a transcriptional start site 70 bp upstream of the lecA translational start codon. A lux box-type element together with RpoS ( S ) consensus sequences was identified upstream of the putative promoter region. In Escherichia coli, expression of a lecA::lux reporter fusion was activated by RhlR/C4-HSL, but not by LasR/3O-C12-HSL, confirming direct regulation by RhlR/C4-HSL. Similarly, in P. aeruginosa PAO1, the expression of a chromosomal lecA::lux fusion was enhanced but not advanced by the addition of exogenous C4-HSL but not 3O-C12-HSL. Furthermore, mutation of rpoS abolished lectin synthesis in P. aeruginosa, demonstrating that both RpoS and RhlR/ C4-HSL are required. Although the C4-HSL-dependent expression of the lecA::lux reporter in E. coli could be inhibited by the presence of 3O-C12-HSL, this did not occur in P. aeruginosa. This suggests that, in the homologous genetic background, 3O-C12-HSL does not function as a posttranslational regulator of the RhlR/ C4-HSL-dependent activation of lecA expression.

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“…The glycolipids containing Gal␣1-4Gal are known as targets on host cells for infections of some pathogenic microbes, e.g. uropathogenic Escherichia coli (9,10), Pseudomonas aeruginosa (PA-I lectin) (11), and Streptococcus suis (12)(13)(14). Bacterial enterotoxins, e.g.…”

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confidence: 99%

Isolation and Characterization of Major Glycoproteins of Pigeon Egg White

Suzuki

Khoo

Chen

et al. 2001

Journal of Biological Chemistry

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Ovotransferrin (POT), two ovalbumins (POA(hi) and POA(lo)), and ovomucoid (POM) were isolated from pigeon egg white (PEW). Unlike their chicken egg white counterparts, PEW glycoproteins contain terminal Gal␣1-4Gal, as evidenced by GS-I lectin (specific for terminal ␣-Gal), anti-P 1 (Gal␣1-4Gal␤1-4GlcNAc␤1-3Gal␤1-4Glc␤1-1Cer) monoclonal antibody, and P fimbriae on uropathogenic Escherichia coli (specific for Gal␣1-4Gal). Gal␣1-4Gal on PEW glycoproteins were found in N-glycans releasable by treatment with glycoamidase F. The respective contents of N-glycans in each glycoprotein were 3.5%, POT; 17%, POA(hi); and 31-37%, POM. POA(hi) has four N-glycosylation sites, in contrast to chicken ovalbumin, which has only one. High performance liquid chromatography analysis showed that N-glycans on POA(hi) were highly heterogeneous. Mass spectrometric analysis revealed that the major N-glycans were monosialylated tri-, tetra-, and penta-antennary oligosaccharides containing terminal Gal␣1-4Gal with or without bisecting N-acetylglucosamine. Oligosaccharide chains terminating in Gal␣1-4Gal are rare among N-glycans from the mammals and avians that have been studied, and our finding is the first predominant presence of (Gal␣1-4Gal)-terminated N-glycans.In mammals, e.g. human, pig, rat, mouse, and hamster, Gal␣1-4Gal is normally found in the terminal and internal positions of glycolipids (1-5), as in P 1 (Gal␣1-4Gal␤1-4GlcNAc␤1-3Gal␤1-4Glc␤1-1Cer), P k (Gal␣1-4Gal␤1-4Glc␤1-1Cer) antigens, and disialosyl galactosyl globoside (NeuAc␣2-3Gal␤1-3(NeuAc␣2-3)GalNAc␤1-3Gal␣1-4Gal␤1-4Glc␤1-1Cer) (6 -8).The glycolipids containing Gal␣1-4Gal are known as targets on host cells for infections of some pathogenic microbes, e.g. uropathogenic Escherichia coli (9, 10), Pseudomonas aeruginosa (PA-I lectin) (11), and Streptococcus suis (12)(13)(14). Bacterial enterotoxins, e.g. from E. coli (verotoxin) (15), Shigella dysenteriae Type 1 (Shiga toxin) (16), and Staphylococcus aureus (enterotoxin B) also specifically bind to these glycolipids (17). In contrast, glycoproteins with Gal␣1-4Gal were found only when the mammals were infected by tapeworm Echnococcus granulosus, in hydatid cyst fluid and membrane caused by the infection (18 -20).However, ovomucoids produced in pigeon (Columba livia) and turtle doves (Streptopelia resoria) possess high level of P 1 antigenic activity (21)(22)(23)(24). Pigeon ovomucoid (POM), 1 one of the major glycoproteins in pigeon egg white (PEW), was also found to bind some pathogenic microbes, e.g. uropathogenic E. coli (24 -26) and S. suis (12)(13)(14). Moreover, POM had been recently utilized for isolation of Shiga-like toxin type 1 (27). Although the presence of Gal␣1-4Gal on ovomucoids of turtle dove and pigeon has been evidenced and these glycoproteins can be utilized for the study of microbiology, complete carbohydrate structures of these ovomucoids are not yet known. Only a tentative structure had been proposed for the main oligosaccharide structure of turtle dove ovomucoid, which includes Gal␣1-4Gal sequence at ...

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PA-I and PA-II lectin interactions with the ABO(H) and P blood group glycosphingolipid antigens may contribute to the broad spectrum adherence ofPseudomonas aeruginosa to human tissues in secondary infections

Cited by 78 publications

References 18 publications

A lipid zipper triggers bacterial invasion

A lipid zipper triggers bacterial invasion

The Pseudomonas aeruginosa Lectins PA-IL and PA-IIL Are Controlled by Quorum Sensing and by RpoS

Isolation and Characterization of Major Glycoproteins of Pigeon Egg White

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