Lipopolysaccharide structures of Helicobacter pylori wild-type strain 26695 and 26695 HP0826::Kan mutant devoid of the O-chain polysaccharide component

Altman, Eleonora; Chandan, Vandana; Li, Jianjun; Vinogradov, Evgeny

doi:10.1016/j.carres.2011.06.036

Cited by 20 publications

(44 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Methylation linkage analysis ( Table A in S1 Text ) indicated a complex monosaccharide composition including terminal and 3-linked Fuc; terminal, 2-, 3- and 4-linked Gal; terminal, 3-, and 6-linked Glc; 2- and 3-linked DD-Hep; 2-, 3-, 7- and 2,7-linked Hep; and terminal, 3-, 4- and 3,4-linked GlcNAc. Overall the monosaccharide composition of wild-type G27 LPS is very similar to the recently re-investigated LPS from strain 26695 [15]. Terminal and 2-linked Gal, and 3,4-linked GlcNAc that are characteristics of the LacNAc element of Lewis antigens were found, together with terminal Fuc, suggesting the existence of both Le x and Le y epitopes that are observed in the LPS of H .…”

Section: Resultssupporting

confidence: 69%

“…Terminal and 2-linked Gal, and 3,4-linked GlcNAc that are characteristics of the LacNAc element of Lewis antigens were found, together with terminal Fuc, suggesting the existence of both Le x and Le y epitopes that are observed in the LPS of H . pylori strains including 26695 [6,7,15–17], SS1 [6,16,32], J99 [6], NCTC11637 [16]. …”

Section: Resultsmentioning

confidence: 99%

“…pylori strain with complete genome sequencing [14], the LPS structure of H . pylori strain 26695 is the most-studied and best-characterized [15–17]. The lipid A and Lewis antigens of H .…”

Section: Introductionmentioning

confidence: 99%

“…The outer core structure of H . pylori 26695 LPS was initially postulated to contain a DD-heptan with the first DD-Hep residue connecting a side-branched α-1,6-glucan [6,16,17,19–22], but a recent reinvestigation into the structure of 26695 LPS revised the outer core as being a linear arrangement of DD-heptan and α-1,6-glucan linked to the inner core through a trisaccharide (GlcNAc-Fuc-DD-Hep) termed as Trio [15] ( Fig 1A ). Furthermore, the attachment site of the O-antigen to the core-oligosaccharide has not been identified [13,15], and therefore the precise assignment of the O-antigen and core-oligosaccharide domains remains unclear.…”

Section: Introductionmentioning

confidence: 99%

“…pylori LPS performed by the research groups of Trent [9,18,23–28], Moran [29–31], Altman [15,19,22,32–35] and Feldman [36,37], the goal of this study was to precisely define the core-oligosaccharide and O-antigen domains. The LPS of the H .…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

The redefinition of Helicobacter pylori lipopolysaccharide O-antigen and core-oligosaccharide domains

Yang

Liao

et al. 2017

PLoS Pathog

View full text Add to dashboard Cite

Helicobacter pylori lipopolysaccharide promotes chronic gastric colonisation through O-antigen host mimicry and resistance to mucosal antimicrobial peptides mediated primarily by modifications of the lipid A. The structural organisation of the core and O-antigen domains of H. pylori lipopolysaccharide remains unclear, as the O-antigen attachment site has still to be identified experimentally. Here, structural investigations of lipopolysaccharides purified from two wild-type strains and the O-antigen ligase mutant revealed that the H. pylori core-oligosaccharide domain is a short conserved hexasaccharide (Glc-Gal-DD-Hep-LD-Hep-LD-Hep-KDO) decorated with the O-antigen domain encompassing a conserved trisaccharide (-DD-Hep-Fuc-GlcNAc-) and variable glucan, heptan and Lewis antigens. Furthermore, the putative heptosyltransferase HP1284 was found to be required for the transfer of the third heptose residue to the core-oligosaccharide. Interestingly, mutation of HP1284 did not affect the ligation of the O-antigen and resulted in the attachment of the O-antigen onto an incomplete core-oligosaccharide missing the third heptose and the adjoining Glc-Gal residues. Mutants deficient in either HP1284 or O-antigen ligase displayed a moderate increase in susceptibility to polymyxin B but were unable to colonise the mouse gastric mucosa. Finally, mapping mutagenesis and colonisation data of previous studies onto the redefined organisation of H. pylori lipopolysaccharide revealed that only the conserved motifs were essential for colonisation. In conclusion, H. pylori lipopolysaccharide is missing the canonical inner and outer core organisation. Instead it displays a short core and a longer O-antigen encompassing residues previously assigned as the outer core domain. The redefinition of H. pylori lipopolysaccharide domains warrants future studies to dissect the role of each domain in host-pathogen interactions. Also enzymes involved in the assembly of the conserved core structure, such as HP1284, could be attractive targets for the design of new therapeutic agents for managing persistent H. pylori infection causing peptic ulcers and gastric cancer.

show abstract

Section: Resultssupporting

confidence: 69%

Section: Resultsmentioning

confidence: 99%

“…pylori strain with complete genome sequencing [14], the LPS structure of H . pylori strain 26695 is the most-studied and best-characterized [15–17]. The lipid A and Lewis antigens of H .…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The redefinition of Helicobacter pylori lipopolysaccharide O-antigen and core-oligosaccharide domains

Yang

Liao

et al. 2017

PLoS Pathog

View full text Add to dashboard Cite

show abstract

The potential of dextran-based glycoconjugates for development of Helicobacter pylori vaccine

2013

View full text Add to dashboard Cite

We have recently demonstrated that synthetic glycoconjugates based on delipidated lipopolysaccharide (LPS) of Helicobacter pylori and containing an α(1-6)-glucan chain induced broadly cross-reactive functional antibodies in immunized animals. To investigate the candidacy of α(1-6)-glucan as an alternative vaccine strategy we prepared glycoconjugates based on dextrans produced by lactic acid bacteria Leuconostoc mesenteroides B512F and consisting of linear α(1-6)-glucan chains with limited branching. Three dextrans with averaged molecular masses of 5,000 Da, 3,500 Da and 1,500 Da, respectively, were modified with a diamino group-containing linker and conjugated to a carrier protein, tetanus toxoid (TT) or diphtheria toxoid (DT), and their immunological properties investigated. The conjugates were immunogenic in both rabbits and mice and induced specific IgG responses against α(1-6)-glucan-expressing H. pylori LPS. Studies performed with post-immune sera of mice and rabbits immunized with dextran-based conjugates demonstrated cross-reactivity with LPS from typeable and non-typeable strains of H. pylori and selected mutants. The post-immune sera from rabbits that received the conjugates exhibited functional activity against α(1-6)-glucan-positive strains of H. pylori. These data provide evidence that dextran-based conjugates may offer a simplified approach to the development of carbohydrate-based vaccines against H. pylori.

show abstract

Helicobacter pylori lipopolysaccharide structural domains and their recognition by immune proteins revealed with carbohydrate microarrays

Silva

Correia

Moreira

et al. 2021

Carbohydrate Polymers

View full text Add to dashboard Cite

Lipopolysaccharide structures of Helicobacter pylori wild-type strain 26695 and 26695 HP0826::Kan mutant devoid of the O-chain polysaccharide component

Cited by 20 publications

References 25 publications

The redefinition of Helicobacter pylori lipopolysaccharide O-antigen and core-oligosaccharide domains

The redefinition of Helicobacter pylori lipopolysaccharide O-antigen and core-oligosaccharide domains

The potential of dextran-based glycoconjugates for development of Helicobacter pylori vaccine

Helicobacter pylori lipopolysaccharide structural domains and their recognition by immune proteins revealed with carbohydrate microarrays

Contact Info

Product

Resources

About