Structural studies of the O-antigen polysaccharides of Klebsiella O5 and Escherichia coli O8

Jansson, Per‐Erik; Lōnngren, Jörgen; Widmalm, Göran; Leontein, Karin; Slettengren, Kerstin; Svenson, Stefan B.; Wrangsell, Göran; Dell, Anne; Tiller, Philip R.

doi:10.1016/s0008-6215(00)90412-9

Cited by 83 publications

(50 citation statements)

References 15 publications

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“…Previous structural analyses of the E. coli O8 PS and the structurally identical Klebsiella O5 PS have shown the presence of O-methyl substitutions at the nonreducing ends of these polymers (13,14). The similarity shared by WbdD O8 and known methyltransferases is consistent with the hypothesis that WbdD modifies the nonreducing end of the growing und-PPlinked O-PS.…”

Section: Conserved Motifs In the Wbdd Proteins Implicate Them In The supporting

confidence: 75%

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Nonreducing Terminal Modifications Determine the Chain Length of Polymannose O Antigens of Escherichia coli and Couple Chain Termination to Polymer Export via an ATP-binding Cassette Transporter

Clarke

Cuthbertson²,

Whitfield

2004

Journal of Biological Chemistry

105

145

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The chain length of bacterial lipopolysaccharide O antigens is regulated to give a modal distribution that is critical for pathogenesis. This paper describes the process of chain length determination in the ATP-binding cassette (ABC) transporter-dependent pathway, a pathway that is widespread among Gram-negative bacteria. Escherichia coli O8 and O9/O9a polymannans are synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the LPS molecule. The polymannan O antigens have nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdD O8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdD O9a catalyzes both reactions, but only the kinase activity controls chain length. Chain termination occurs in a mutant lacking the ABC transporter, indicating that it precedes export. An E. coli wbdD O9a mutant accumulated O9a polymannan in the cytoplasm, indicating that WbdD activity coordinates polymannan chain termination with export across the inner membrane.

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Section: Conserved Motifs In the Wbdd Proteins Implicate Them In The supporting

confidence: 75%

“…1). The polymannans have nonreducing terminal O-methyl groups (13,14). Identical O-PS structures and gene clusters are found in Klebsiella pneumoniae O3 (E. coli O9) and K. pneumoniae O5 (E. coli O8) as a result of lateral gene transfer (15).…”

mentioning

confidence: 99%

Nonreducing Terminal Modifications Determine the Chain Length of Polymannose O Antigens of Escherichia coli and Couple Chain Termination to Polymer Export via an ATP-binding Cassette Transporter

Clarke

Cuthbertson²,

Whitfield

2004

Journal of Biological Chemistry

105

145

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“…Mannan-coated ELISA plates were kindly provided by Wieslab AB. We also examined LPS from 3 mannose-rich E. coli strains, E. coli O8 (47), E. coli O44 (48), and E. coli O77 (49).…”

Section: Discussionmentioning

confidence: 99%

Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2

Selander

Mårtensson

Weintraub

et al. 2006

Journal of Clinical Investigation

164

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Lectin pathway activation of C3 is known to involve target recognition by mannan-binding lectin (MBL)or ficolins and generation of classical pathway C3 convertase via cleavage of C4 and C2 by MBL-associated serine protease 2 (MASP-2). We investigated C3 activation in C2-deficient human sera and in sera with other defined defects of complement to assess other mechanisms through which MBL might recruit complement. The capacity of serum to support C3 deposition was examined by ELISA using microtiter plates coated with O antigen-specific oligosaccharides derived from Salmonella typhimurium, S. thompson, and S. enteritidis corresponding to serogroups B, C, and D (BO, CO, and DO). MBL bound to CO, but not to BO and DO, and efficiently supported C3 deposition in the absence of C2, C4, or MASP-2. The existence of an MBL-dependent C2 bypass mechanism for alternative pathway-mediated C3 activation was clearly demonstrated using CO, solid-phase mannan, and E. coli LPS. MASP-1 might contribute, but was not required for C3 deposition in the model used. Independent of MBL, specific antibodies to CO supported C3 deposition through classical and alternative pathways. MBL-dependent C2 bypass activation could be particularly important in various inherited and acquired complement deficiency states.

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“…To date it is still unknown how the chain length of O-PS is controlled in the ABC transporter-dependent pathway (reviewed in reference 53). In the E. coli O8 antigen (the synthesis of which is similar to that of O9a), polymannose chains terminate in 3-O-methylmannose, and this has been proposed to reflect a discrete termination process (15). The biosynthetic source of the modified mannosyl residue is unknown.…”

Section: Discussionmentioning

confidence: 99%

Functional Analysis of the Galactosyltransferases Required for Biosynthesis of d -Galactan I, a Component of the Lipopolysaccharide O1 Antigen of Klebsiella pneumoniae

2001

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(Fig. 1B). D-Galactan II provides the epitope or epitopes that define the O1 antigen (55). The presence of D-galactan II is required for the resistance of the bacteria to complement-mediated killing in the host, and therefore Klebsiella pneumoniae mutants that produce only D-galactan I are serum sensitive (33).There are two major pathways for the biosynthesis of LPS O-PS. These are designated Wzy dependent and ATP-binding cassette (ABC) transporter dependent (reviewed in references 52 and 53). Both pathways are widely distributed among different genera and are involved in the synthesis of diverse O-PS structures. A third pathway (synthase dependent) is currently confined to a single O-PS (17). In the Wzy-dependent mechanism, undecaprenyl pyrophosphoryl (und-PP)-linked oligosaccharide repeat units are assembled at the cytoplasmic face of the inner membrane. These intermediates are then exported to the periplasmic face, where they provide the direct substrates for polymerization. Export and polymerization require the activity of members of the Wzx and Wzy protein families, respectively. In the ABC transporter-dependent mechanism, the polymer is built by processive transfer of glycosyl residues to an initiating und-PP-linked lipid intermediate at the cytoplasmic face of the inner membrane. After the lipid-linked polymer is synthesized at the cytoplasmic face of the inner membrane, it is exported to the periplasmic face by an ABC transporter (5, 45, 58). The various O-PS biosynthesis pathways are believed to converge with the presence of und-PPlinked polymer at the periplasmic face of the inner membrane, at which point the nascent O-PS is ligated to preformed lipid A core. The completed LPS molecule is then translocated to the outer leaflet of the outer membrane by a process that is still undetermined.In members of the family Enterobacteriaceae, initiation of ABC transporter-dependent

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Structural studies of the O-antigen polysaccharides of Klebsiella O5 and Escherichia coli O8

Cited by 83 publications

References 15 publications

Nonreducing Terminal Modifications Determine the Chain Length of Polymannose O Antigens of Escherichia coli and Couple Chain Termination to Polymer Export via an ATP-binding Cassette Transporter

Nonreducing Terminal Modifications Determine the Chain Length of Polymannose O Antigens of Escherichia coli and Couple Chain Termination to Polymer Export via an ATP-binding Cassette Transporter

Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2

Functional Analysis of the Galactosyltransferases Required for Biosynthesis of d -Galactan I, a Component of the Lipopolysaccharide O1 Antigen of Klebsiella pneumoniae

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