Literature DB >> 17662691

The Hd0053 gene of Haemophilus ducreyi encodes an alpha2,3-sialyltransferase.

Yanhong Li1, Mingchi Sun, Shengshu Huang, Hai Yu, Harshal A Chokhawala, Vireak Thon, Xi Chen.   

Abstract

Haemophilus ducreyi is a Gram-negative bacterium that causes chancroid, a sexually transmitted genital ulcer disease. Different lipooligosaccharide (LOS) structures have been identified from H. ducreyi strain 35000, including those sialylated glycoforms. Surface LOS of H. ducreyi is considered an important virulence factor that is involved in ulcer formation, cell adhesion, and invasion of host tissue. Gene Hd0686 of H. ducreyi, designated lst (for lipooligosaccharide sialyltransferase), was identified to encode an alpha2,3-sialyltransferase that is important for the formation of sialylated LOS. Here, we show that Hd0053 of H. ducreyi genomic strain 35000HP, the third member of the glycosyltransferase family 80 (GT80), also encodes an alpha2,3-sialyltransferase that may be important for LOS sialylation.

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Year:  2007        PMID: 17662691      PMCID: PMC2084346          DOI: 10.1016/j.bbrc.2007.07.063

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  30 in total

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Journal:  J Biol Chem       Date:  2002-02-12       Impact factor: 5.157

5.  Biosynthesis of sialylated lipooligosaccharides in Haemophilus ducreyi is dependent on exogenous sialic acid and not mannosamine. Incorporation studies using N-acylmannosamine analogues, N-glycolylneuraminic acid, and 13C-labeled N-acetylneuraminic acid.

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6.  CpsK of Streptococcus agalactiae exhibits alpha2,3-sialyltransferase activity in Haemophilus ducreyi.

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7.  Host-derived sialic acid is incorporated into Haemophilus influenzae lipopolysaccharide and is a major virulence factor in experimental otitis media.

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9.  Incorporation of N-acetylneuraminic acid into Haemophilus somnus lipooligosaccharide (LOS): enhancement of resistance to serum and reduction of LOS antibody binding.

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Journal:  Infect Immun       Date:  2002-09       Impact factor: 3.441

10.  Identification of a bifunctional lipopolysaccharide sialyltransferase in Haemophilus influenzae: incorporation of disialic acid.

Authors:  Kate L Fox; Andrew D Cox; Michel Gilbert; Warren W Wakarchuk; Jianjun Li; Katherine Makepeace; James C Richards; E Richard Moxon; Derek W Hood
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  8 in total

1.  Sialylation of lipooligosaccharides is dispensable for the virulence of Haemophilus ducreyi in humans.

Authors:  Stanley M Spinola; Wei Li; Kate R Fortney; Diane M Janowicz; Beth Zwickl; Barry P Katz; Robert S Munson
Journal:  Infect Immun       Date:  2011-12-05       Impact factor: 3.441

2.  PmST2: a novel Pasteurella multocida glycolipid α2-3-sialyltransferase.

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Journal:  Glycobiology       Date:  2011-04-21       Impact factor: 4.313

3.  N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela alpha2,6-sialyltransferase.

Authors:  Mingchi Sun; Yanhong Li; Harshal A Chokhawala; Ryan Henning; Xi Chen
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Review 4.  Advances in the biology and chemistry of sialic acids.

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Journal:  ACS Chem Biol       Date:  2010-02-19       Impact factor: 5.100

5.  Converting Pasteurella multocidaα2-3-sialyltransferase 1 (PmST1) to a regioselective α2-6-sialyltransferase by saturation mutagenesis and regioselective screening.

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Journal:  Org Biomol Chem       Date:  2017-01-30       Impact factor: 3.876

Review 6.  Sialic acid metabolism and sialyltransferases: natural functions and applications.

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Journal:  Appl Microbiol Biotechnol       Date:  2012-04-13       Impact factor: 4.813

7.  Multifunctionality of Campylobacter jejuni sialyltransferase CstII: characterization of GD3/GT3 oligosaccharide synthase, GD3 oligosaccharide sialidase, and trans-sialidase activities.

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  8 in total

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