Identification and characterization of a lipopolysaccharide α,2,3-sialyltransferase from the human pathogen Helicobacter bizzozeronii

Pradeep Kumar Kondadi, Mirko Rossi, Brigitte Twelkmeyer, Melissa J Schur, Jianjun Li, Thomas Schott, Lars Paulin, Petri Auvinen, Marja-Liisa Hänninen, Elke K H Schweda, Warren Wakarchuk

Research output: Contribution to journalArticleScientificpeer-review

Abstract

Terminal sialic acid in the lipopolysaccharide (LPS) 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 H. 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 mono-functional α2,3-sialyltransferase activity with a preference for N-acetyllactosamine as a substrate. The LPSs from different strains were shown by SDS-PAGE and HPAEC-PAD to contain sialic acid after neuraminidase treatment. The expression of this sialyltransferase and sialyl-LPS appeared to be a common phase variable characteristic between 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-LewisX 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.

Original languageEnglish
JournalJournal of Bacteriology
Volume194
Issue number10
Pages (from-to)2540-2550
Number of pages11
ISSN0021-9193
DOIs
Publication statusPublished - 2012
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 413 Veterinary science
  • HELICOBACTER BIZZOZERONII
  • sialyltransferases
  • sialyl-lactoseamine
  • PHYLOGENY
  • LIPOPOLYSACCHARIDES

Cite this

Kondadi, Pradeep Kumar ; Rossi, Mirko ; Twelkmeyer, Brigitte ; Schur, Melissa J ; Li, Jianjun ; Schott, Thomas ; Paulin, Lars ; Auvinen, Petri ; Hänninen, Marja-Liisa ; Schweda, Elke K H ; Wakarchuk, Warren. / Identification and characterization of a lipopolysaccharide α,2,3-sialyltransferase from the human pathogen Helicobacter bizzozeronii. In: Journal of Bacteriology. 2012 ; Vol. 194, No. 10. pp. 2540-2550.
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title = "Identification and characterization of a lipopolysaccharide α,2,3-sialyltransferase from the human pathogen Helicobacter bizzozeronii",
abstract = "Terminal sialic acid in the lipopolysaccharide (LPS) 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 H. 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 mono-functional α2,3-sialyltransferase activity with a preference for N-acetyllactosamine as a substrate. The LPSs from different strains were shown by SDS-PAGE and HPAEC-PAD to contain sialic acid after neuraminidase treatment. The expression of this sialyltransferase and sialyl-LPS appeared to be a common phase variable characteristic between 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-LewisX 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.",
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author = "Kondadi, {Pradeep Kumar} and Mirko Rossi and Brigitte Twelkmeyer and Schur, {Melissa J} and Jianjun Li and Thomas Schott and Lars Paulin and Petri Auvinen and Marja-Liisa H{\"a}nninen and Schweda, {Elke K H} and Warren Wakarchuk",
year = "2012",
doi = "10.1128/JB.00126-12",
language = "English",
volume = "194",
pages = "2540--2550",
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Identification and characterization of a lipopolysaccharide α,2,3-sialyltransferase from the human pathogen Helicobacter bizzozeronii. / Kondadi, Pradeep Kumar; Rossi, Mirko; Twelkmeyer, Brigitte; Schur, Melissa J; Li, Jianjun; Schott, Thomas; Paulin, Lars; Auvinen, Petri; Hänninen, Marja-Liisa; Schweda, Elke K H; Wakarchuk, Warren.

In: Journal of Bacteriology, Vol. 194, No. 10, 2012, p. 2540-2550.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Identification and characterization of a lipopolysaccharide α,2,3-sialyltransferase from the human pathogen Helicobacter bizzozeronii

AU - Kondadi, Pradeep Kumar

AU - Rossi, Mirko

AU - Twelkmeyer, Brigitte

AU - Schur, Melissa J

AU - Li, Jianjun

AU - Schott, Thomas

AU - Paulin, Lars

AU - Auvinen, Petri

AU - Hänninen, Marja-Liisa

AU - Schweda, Elke K H

AU - Wakarchuk, Warren

PY - 2012

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N2 - Terminal sialic acid in the lipopolysaccharide (LPS) 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 H. 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 mono-functional α2,3-sialyltransferase activity with a preference for N-acetyllactosamine as a substrate. The LPSs from different strains were shown by SDS-PAGE and HPAEC-PAD to contain sialic acid after neuraminidase treatment. The expression of this sialyltransferase and sialyl-LPS appeared to be a common phase variable characteristic between 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-LewisX 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.

AB - Terminal sialic acid in the lipopolysaccharide (LPS) 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 H. 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 mono-functional α2,3-sialyltransferase activity with a preference for N-acetyllactosamine as a substrate. The LPSs from different strains were shown by SDS-PAGE and HPAEC-PAD to contain sialic acid after neuraminidase treatment. The expression of this sialyltransferase and sialyl-LPS appeared to be a common phase variable characteristic between 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-LewisX 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.

KW - 413 Veterinary science

KW - HELICOBACTER BIZZOZERONII

KW - sialyltransferases

KW - sialyl-lactoseamine

KW - PHYLOGENY

KW - LIPOPOLYSACCHARIDES

U2 - 10.1128/JB.00126-12

DO - 10.1128/JB.00126-12

M3 - Article

VL - 194

SP - 2540

EP - 2550

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 10

ER -