A Haemophilus influenzae strain associated with Fisher syndrome expresses a novel disialylated ganglioside mimic: Biochemistry

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TypeArticle
Journal titleBiochemistry
Volume46
Issue27
Pages81648171; # of pages: 8
SubjectACID; ACID RESIDUES; Adult; Antibodies; antibody; backbone; Canada; Carbohydrate Sequence; GANGLIOSIDE; Gangliosides; Haemophilus; Haemophilus influenzae; HAEMOPHILUS-INFLUENZAE; Humans; lipooligosaccharide; Magnetic Resonance Spectroscopy; Male; mass spectrometry; metabolism; Microbiology; Miller Fisher Syndrome; Molecular Mimicry; Molecular Sequence Data; physiology; RESIDUES; Serum; SIALIC; SIALIC-ACID; STRAIN; surface; Syndrome; TARGET; TRISACCHARIDE
AbstractThe non-typeable Haemophilus influenzae strain DH1 was isolated from a 25 year old male patient with Fisher syndrome, a postinfectious autoimmune condition characterized by the presence of anti-GQ1b IgG antibodies that target and initiate damage to peripheral nerves. DH1 was found to display an alphaNeuAc(2-8)alphaNeuAc(2-3)betaGal branch bound to the tetraheptosyl backbone core of its lipooligosaccharide (LOS). The novel sialylation pattern was found to be dependent on the activity of a bifunctional sialyltransferase, Lic3B, which catalyzes the addition of both the terminal and subterminal sialic acid residues. Patient serum IgGs bind to DH1 LOS, and the reactivity is significantly influenced by the presence of sialylated glycoforms. The display by DH1, of a surface glycan that mimics the terminal trisaccharide portion of disialosyl-containing gangliosides, provides strong evidence for its involvement in the development of Fisher syndrome
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberHOULISTON2007
NPARC number9387155
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Record identifiere8ac8f4a-4a42-45ad-a528-92ba9d338cae
Record created2009-07-10
Record modified2016-05-09
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