Hug et al., 2010 - Google Patents
Helicobacter pylori lipopolysaccharide is synthesized via a novel pathway with an evolutionary connection to protein N-glycosylationHug et al., 2010
View HTML- Document ID
- 13718982697716451514
- Author
- Hug I
- Couturier M
- Rooker M
- Taylor D
- Stein M
- Feldman M
- Publication year
- Publication venue
- PLoS pathogens
External Links
Snippet
Lipopolysaccharide (LPS) is a major component on the surface of Gram negative bacteria and is composed of lipid A-core and the O antigen polysaccharide. O polysaccharides of the gastric pathogen Helicobacter pylori contain Lewis antigens, mimicking glycan structures …
- 239000002158 endotoxin 0 title abstract description 110
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1051—Hexosyltransferases (2.4.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/02—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving viable micro-organisms
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Hug et al. | Helicobacter pylori lipopolysaccharide is synthesized via a novel pathway with an evolutionary connection to protein N-glycosylation | |
Edwards et al. | Lewis X structures in the O antigen side‐chain promote adhesion of Helicobacter pylori to the gastric epithelium | |
Wang et al. | Molecular genetic basis for the variable expression of Lewis Y antigen in Helicobacter pylori: analysis of the α (1, 2) fucosyltransferase gene | |
Linton et al. | Functional analysis of the Campylobacter jejuni N‐linked protein glycosylation pathway | |
Kelly et al. | Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer | |
Dell et al. | Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes | |
Szymanski et al. | Protein glycosylation in bacterial mucosal pathogens | |
Tailford et al. | Mucin glycan foraging in the human gut microbiome | |
Appelmelk et al. | Phase variation in Helicobacter pylori lipopolysaccharide due to changes in the lengths of poly (C) tracts in α3-fucosyltransferase genes | |
Van Sorge et al. | N‐glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C‐type lectin receptor MGL | |
Nishiyama et al. | Bifidobacterium bifidum extracellular sialidase enhances adhesion to the mucosal surface and supports carbohydrate assimilation | |
Hug et al. | Analogies and homologies in lipopolysaccharide and glycoprotein biosynthesis in bacteria | |
Nothaft et al. | Protein glycosylation in bacteria: sweeter than ever | |
Lees‐Miller et al. | A common pathway for O‐linked protein‐glycosylation and synthesis of capsule in A cinetobacter baumannii | |
Karlyshev et al. | The Campylobacter jejuni glycome | |
Bengoechea et al. | Functional characterization of Gne (UDP-N-acetylglucosamine-4-epimerase), Wzz (chain length determinant), and Wzy (O-antigen polymerase) of Yersinia enterocolitica serotype O: 8 | |
Hartley et al. | Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N, N′-diacetylbacillosamine | |
Phansopa et al. | Structural and functional characterization of NanU, a novel high-affinity sialic acid-inducible binding protein of oral and gut-dwelling Bacteroidetes species | |
Abeyrathne et al. | WaaL of Pseudomonas aeruginosa utilizes ATP in in vitro ligation of O antigen onto lipid A‐core | |
Fox et al. | Identification of a bifunctional lipopolysaccharide sialyltransferase in Haemophilus influenzae: incorporation of disialic acid | |
Cain et al. | Identifying the targets and functions of N-linked protein glycosylation in Campylobacter jejuni | |
Bartels et al. | Glycosylation is required for outer membrane localization of the lectin LecB in Pseudomonas aeruginosa | |
Langdon et al. | N-linked glycosylation in bacteria: an unexpected application | |
Steiner et al. | Functional characterization of the initiation enzyme of S-layer glycoprotein glycan biosynthesis in Geobacillus stearothermophilus NRS 2004/3a | |
Moulton et al. | Metabolic glycan labeling-based screen to identify bacterial glycosylation genes |