Secondary sugar binding site identified for LecA lectin from <i>Pseudomonas aeruginosa</i>

Blanchard, Bertrand; Imberty, Anne; Varrot, A.

doi:10.1002/prot.24430

Cited by 19 publications

(24 citation statements)

References 25 publications

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“…LecA has been shown to specifically bind to galactose or glucose, while LecB binds specifically to fucose or mannose. 38,39 In addition the type IV pili of P. aeruginosa can bind to the b-Nacetylgalactosamine (1-4)-b-galactose via the pilus subunit PilA. Staphylococcus aureus strains can produce various capsular polysaccharides that can coat their surface, and these capsules can contain N-acetylgalactosaminuronic acid, Nacetyl-D-fucosamine, N-acetyl-D-glucosaminuronic acid, and N-acetylmannosaminuronic acid, 40 which may represent the ligands for the P. aeruginosa protein(s).…”

Section: Discussionmentioning

confidence: 99%

Bacterial Coaggregation Among the Most Commonly Isolated Bacteria From Contact Lens Cases

Datta

Stapleton

Willcox

2017

Invest. Ophthalmol. Vis. Sci.

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PURPOSE. To examine the coaggregation and cohesion between the commonly isolated bacteria from contact lens cases.METHODS. Four or five strains each of commonly isolated bacteria from contact lens cases, Staphylococcus aureus, Staphylococcus epidermidis, Pseudomonas aeruginosa, and Serratia marcescens, were grown, washed, mixed in equal proportions, and allowed to coaggregate for 24 hours. Lactose (0.06 M), sucrose (0.06 M), and pronase (2 mg/mL; 2 hours, 378C) were used to inhibit coaggregation. Oral bacterial isolates of Actinomyces naeslundii and Streptococcus sanguinis were used as a positive control for coaggregation. Cohesion was performed with the ocular bacteria that demonstrated the highest level of coaggregation. Production of growth-inhibitory substances was measured by growing strains together on agar plates. RESULTS.The oral bacterial pair showed >80% coaggregation. Coaggregation occurred between ocular strains of S. aureus (2/5) or S. epidermidis (2/5) with P. aeruginosa strains (3/5); 42% to 62%. There was only slight coaggregation between staphylococci and S. marcescens. Staphylococcus aureus coaggregated with S. epidermidis. Lactose or sucrose treatment of S. aureus but pronase treatment of P. aeruginosa reversed the coaggregation. There was no cohesion between the ocular isolates. P. aeruginosa was able to stop growth of S. aureus but not vice versa.CONCLUSIONS. This study demonstrated for the first time that ocular isolates of P. aeruginosa and S. aureus could coaggregate, probably through lectin-carbohydrate interactions. However, this may not be related to biofilm formation in contact lens cases, as there was no evidence that the coaggregation was associated with cohesion between the strains.

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Section: Discussionmentioning

confidence: 99%

Bacterial Coaggregation Among the Most Commonly Isolated Bacteria From Contact Lens Cases

Datta

Stapleton

Willcox

2017

Invest. Ophthalmol. Vis. Sci.

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“…A lecA mutant of PAO1 exhibits reduced substratum coverage while a LecA-overproducing strain exhibits increased biofilm formation (7). LecA binds to galactose, N -acetyl-D-galactosamine and glucose (60, 78). It is yet to be determined if LecA binds to the galactose-rich Psl and glucose-rich Pel; such an interaction would contribute to biofilm formation.…”

Section: Leca and Lecb Lectinsmentioning

confidence: 99%

“…In the LecA structure, each monomer adopts a small jelly-roll β-sandwich fold, consisting of two curved sheets, with a calcium-dependent ligand binding site at the apex that binds one galactose ligand and one calcium ion (85). LecA also contains a secondary glucose-binding site in close proximity to the primary galactose-binding site, but the bound glucose residue does not interact with the amino acid residues of the galactose-binding site (78). LecA-mediated biofilm formation involves the galactose binding site.…”

Section: Leca and Lecb Lectinsmentioning

confidence: 99%

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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“…PA-IL has similar characteristics as AJLec in its folds (small jelly-roll type β-sandwich folds), function (galactose-binding in a Ca 2+ ion-dependent manner), and positions of sugar-binding sites in protomer structures (Fig. 3E ) 21 . On the other hand, there was no homology observed in amino acid sequences, structures in sugar-binding sites, and quaternary structures (AJLec, dimer; PA-IL, tetramer) between AJLec and PA-IL.…”

Section: Discussionmentioning

confidence: 88%

Identification, Characterization, and X-ray Crystallographic Analysis of a Novel Type of Lectin AJLec from the Sea Anemone Anthopleura japonica

Unno

Nakamura

Mori

et al. 2018

Sci Rep

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A novel galactose-specific lectin, AJLec (18.5 kDa), was isolated from the sea anemone, Anthopleura japonica. AJLec was characterized using the hemagglutination assay, isothermal titration calorimetry (ITC), and glycoconjugate microarray analysis and we found that AJLec has a specificity for galactose monomers and β-linked terminal galactose residues in complex carbohydrates, but not for N-acetylgalactosamine (GalNAc), which is commonly recognized by galactose-binding lectins. The primary structure of AJLec did not show homology with known lectins, and a crystal structural analysis also revealed a unique homodimeric structure. The crystal structure of AJLec complexed with lactose was solved by measuring the sulfur single-wavelength anomalous diffraction (S-SAD) phasing with an in-house Cu Kα source method. This analysis revealed that the galactose residue in lactose was recognized via its O2, O3, and O4 hydroxyl groups and ring oxygen by calcium coordination and two hydrogen bonds with residues in the carbohydrate-binding site, which demonstrated strict specificity for the β-linked terminal galactose in this lectin.

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Secondary sugar binding site identified for LecA lectin from Pseudomonas aeruginosa

Cited by 19 publications

References 25 publications

Bacterial Coaggregation Among the Most Commonly Isolated Bacteria From Contact Lens Cases

Bacterial Coaggregation Among the Most Commonly Isolated Bacteria From Contact Lens Cases

Biofilm Matrix Proteins

Identification, Characterization, and X-ray Crystallographic Analysis of a Novel Type of Lectin AJLec from the Sea Anemone Anthopleura japonica

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