Occurrence of a common lipopolysaccharide antigen in standard and clinical strains of Pseudomonas aeruginosa

Lam, M. Y. C.; McGroarty, Estelle J.; Kropinski, Andrew M.; MacDonald, Leslie A.; Pedersen, Susanne Juhl; Høiby, Niels; Lam, Joseph S.

doi:10.1128/jcm.27.5.962-967.1989

Cited by 138 publications

(109 citation statements)

References 26 publications

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“…Only one series (Bbands) reacted in immunoblotting with monoclonal antibodies specific to the O-antigen. Another monoclonal antibody specific to A-bands revealed the presence of A-series in LPS from 11 of 17 standard serotype strains of the International Antigenic Typing Scheme of P. aeruginosa and 170 of 250 clinical isolates from patients with cystic fibrosis [20]. Taking into account our present data, one can assume that the A-bands described in [19,20] correspond to LPS molecules with CPA chain.…”

Section: Discussionsupporting

confidence: 53%

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Detection of common polysaccharide antigen of Pseudomonas aeruginosa with O-antiserum to Pseudomonas cerasi

Kocharova

1991

FEMS Microbiology Letters

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Section: Discussionsupporting

confidence: 53%

“…It is noteworthy that two series of ladder-like bands (A and B) were observed in gel when LPS preparation from P. aeruginosa PAO1 was subjected to SDS-PAGE [19,20]. Only one series (Bbands) reacted in immunoblotting with monoclonal antibodies specific to the O-antigen.…”

Section: Discussionmentioning

confidence: 99%

Detection of common polysaccharide antigen of Pseudomonas aeruginosa with O-antiserum to Pseudomonas cerasi

Kocharova

1991

FEMS Microbiology Letters

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“…It was shown by Kuzio and Kropinski [7] that the 13 C-NMR spectrum of the O-chain polysaccharide from strain PAO1 was identical to that of P. aeruginosa Lanyi O:3a,3d polysaccharide [8,9]. We have recently reported the structural elucidation of the complete core region of P. aeruginosa serotypes O5 and O6 LPS [6,10,11]. In the present investigation, an extended core containing one repeating unit, present in both O-chaindeficient mutants and in the wild-type strain PAO1, was used to determine the O-chain linkage region of LPS from P. aeruginosa serotype O5.…”

mentioning

confidence: 94%

“…In addition, these strains will have LPS that is devoid of O-polysaccharide [rough (R)-type LPS] and LPS containing only one O-chain repeating unit [semi-rough (SR)-type LPS]. P. aeruginosa isolates from patients with cystic fibrosis have been shown to be deficient in O-antigenic long-chain LPS [5], and its progressive loss in the clinical isolates collected from cystic fibrosis patients over a number of years has been reported [6]. The complete and exact knowledge of LPS structure is necessary for better understanding of its immunochemistry and biosynthesis, and for providing a molecular basis for the development of therapeutic intervention strategies in P. aeruginosa infections.…”

mentioning

confidence: 99%

Structural characterization of the outer core and the O‐chain linkage region of lipopolysaccharide from Pseudomonas aeruginosa serotype O5

Sadovskaya

Brisson

Thibault

et al. 2000

European Journal of Biochemistry

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The point of attachment of the O-chain in the outer core region of Pseudomonas aeruginosa serotype O5 lipopolysaccharide (LPS) was determined following a detailed analysis of the extended core oligosaccharide, containing one trisaccharide O-chain repeating unit, present in both the wild-type strain PAO1 and O-chain deficient mutant strains AK1401 and PAO-rfc. The structure of the extended core oligosaccharide was determined by various mass spectrometric methods as well as one-dimensional and two-dimensional NMR spectroscopy. Furthermore, the one-dimensional analogues of NOESY and TOCSY experiments were applied to confirm the structure of the outer core region in the O-chain polysaccharide. In both the extended core oligosaccharide and the core of the smooth LPS, a loss of one of the b-glucosyl residues and the translocation of the a-rhamnosyl residue, followed by the attachment of the first O-chain repeating unit was observed. This process is complicated and could involve two distinct rhamnosyltransferases, one with a-1,6-linkage specificity and another with a-1,3-linkage specificity. It is also plausible that an a-1,3 rhamnosyltransferase facilitates the addition of thè new' a-rhamnosyl residue that will act as a receptor for the attachment of the single O-antigen repeating unit in the LPS of the semi-rough mutant. The 2-amino-2-deoxy-fucosyl residue of the first O-chain repeating unit directly attached to the core was found to have a b-anomeric configuration instead of an a configuration, characteristic for this residue as a component of the O-chain polysaccharide. The results of this study provide the first example of the mechanistic implications of the structure of the outer core region in a fully assembled O-chain containing LPS, differing from the O-chain deficient rough LPS.

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“…A-band O polysaccharide is apparently immunologically invisible to the host in the initial stages of infection, but becomes a major antigen over time as other LPS forms are selectively lost. The appearance of antibodies against A band in host serum correlates with extended duration of disease and reduced lung function [20].…”

mentioning

confidence: 99%

The structural basis for catalytic function of GMD and RMD, two closely related enzymes from the GDP‐d‐rhamnose biosynthesis pathway

et al. 2009

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The rare 6-deoxysugar d-rhamnose is a component of bacterial cell surface glycans, including the d-rhamnose homopolymer produced by Pseudomonas aeruginosa, called A-band O polysaccharide. GDP-d-rhamnose synthesis from GDP-d-mannose is catalyzed by two enzymes. The first is a GDP-d-mannose-4,6-dehydratase (GMD). The second enzyme, RMD, reduces the GMD product (GDP-6-deoxy-d-lyxo-hexos-4-ulose) to GDP-d-rhamnose. Genes encoding GMD and RMD are present in P. aeruginosa, and genetic evidence indicates they act in A-band O-polysaccharide biosynthesis. Details of their enzyme functions have not, however, been previously elucidated. We aimed to characterize these enzymes biochemically, and to determine the structure of RMD to better understand what determines substrate specificity and catalytic activity in these enzymes. We used capillary electrophoresis and NMR analysis of reaction products to precisely define P. aeruginosa GMD and RMD functions. P. aeruginosa GMD is bifunctional, and can catalyze both GDP-d-mannose 4,6-dehydration and the subsequent reduction reaction to produce GDP-d-rhamnose. RMD catalyzes the stereospecific reduction of GDP-6-deoxy-d-lyxo-hexos-4-ulose, as predicted. Reconstitution of GDP-d-rhamnose biosynthesis in vitro revealed that the P. aeruginosa pathway may be regulated by feedback inhibition in the cell. We determined the structure of RMD from Aneurinibacillus thermoaerophilus at 1.8 Å resolution. The structure of A. thermoaerophilus RMD is remarkably similar to that of P. aeruginosa GMD, which explains why P. aeruginosa GMD is also able to catalyze the RMD reaction. Comparison of the active sites and amino acid sequences suggests that a conserved amino acid side chain (Arg185 in P. aeruginosa GMD) may be crucial for orienting substrate and cofactor in GMD enzymes.

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Occurrence of a common lipopolysaccharide antigen in standard and clinical strains of Pseudomonas aeruginosa

Cited by 138 publications

References 26 publications

Detection of common polysaccharide antigen of Pseudomonas aeruginosa with O-antiserum to Pseudomonas cerasi

Detection of common polysaccharide antigen of Pseudomonas aeruginosa with O-antiserum to Pseudomonas cerasi

Structural characterization of the outer core and the O‐chain linkage region of lipopolysaccharide from Pseudomonas aeruginosa serotype O5

The structural basis for catalytic function of GMD and RMD, two closely related enzymes from the GDP‐d‐rhamnose biosynthesis pathway

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