| DOI | Resolve DOI: https://doi.org/10.1128/JB.00126-12 |
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| Author | Search for: Kondadi, P.K.; Search for: Rossi, M.; Search for: Twelkmeyer, B.; Search for: Schur, M.J.1; Search for: Li, J.1; Search for: Schott, T.; Search for: Paulin, L.; Search for: Auvinen, P.; Search for: Hänninen, M.-L.; Search for: Schweda, E.K.H.; Search for: Wakarchuk, W.1 |
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| Affiliation | - National Research Council of Canada. NRC Institute for Biological Sciences
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| Format | Text, Article |
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| Subject | alpha, 2,3 sialyltransferase; bacterial enzyme; bacterium lipopolysaccharide; n acetylneuraminic acid; sialic acid; sialidase; sialyl Lewis x antigen; sialyltransferase; unclassified drug; anion exchange chromatography; bacterial genome; bacterial strain; bacterium isolate; carbohydrate synthesis; gene sequence; Helicobacter; Helicobacter bizzozeronii; nucleotide sequence; polyacrylamide gel electrophoresis; protein expression; sialylation; Antibodies, Bacterial; Cholera Toxin; Dogs; Gene Expression Regulation, Bacterial; Genome, Bacterial; Helicobacter; Lipopolysaccharides; Molecular Sequence Data; Multigene Family; Phylogeny; Recombinant Proteins; Sialyltransferases; Canis familiaris; Helicobacter; Helicobacter bizzozeronii; Mammalia |
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| Abstract | Terminal sialic acid in the lipopolysaccharides (LPSs) of mucosal pathogens is an important virulence factor. Here we report the characterization of a Helicobacter sialyltransferase involved in the biosynthesis of sialylated LPS in Helicobacter bizzozeronii, the only non-pylori gastric Helicobacter species isolated from humans thus far. Starting from the genome sequences of canine and human strains, we identified potential sialyltransferases downstream of three genes involved in the biosynthesis of N-acetylneuraminic acid. One of these candidates showed monofunctional α,2,3-sialyltransferase activity with a preference for N-acetyllactosamine as a substrate. The LPSs from different strains were shown by SDS-PAGE and high-performance anionexchange chromatography with pulsed amperometric detection (HPAEC-PAD) to contain sialic acid after neuraminidase treatment. The expression of this sialyltransferase and sialyl-LPS appeared to be a phase-variable characteristic common to both human and canine H. bizzozeronii strains. The sialylation site of the LPSs of two H. bizzozeronii strains was determined to be NeuAc-Hex-HexNAc, suggesting terminal 3'-sialyl-LacNAc. Moreover, serological typing revealed the possible presence of sialyl-Lewis X in two additional strains, indicating that H. bizzozeronii could also mimic the surface glycans of mammalian cells. The expression of sialyl-glycans may influence the adaptation process of H. bizzozeronii during the host jump from dogs to humans. © 2012, American Society for Microbiology. |
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| Publication date | 2012 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21269319 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 94cbe54f-c12d-4664-8f68-dab3dd12bf51 |
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| Record created | 2013-12-12 |
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| Record modified | 2020-04-21 |
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