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

Abstract

The 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.

• Authors: R Scott Houliston, Michiaki Koga, Jianjun Li, Harold C Jarrell, James C Richards, Varvara Vitiazeva, Elke K H Schweda, Nobuhiro Yuki, Michel Gilbert
• Journal: Biochemistry (Biochemistry) Vol. 46 Issue 27 Pg. 8164-71 (Jul 10 2007) ISSN: 0006-2960 [Print] United States
• PMID: 17567050 (Publication Type: Case Reports, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Gangliosides

Topics

• Adult
• Carbohydrate Sequence
• Gangliosides (metabolism)
• Haemophilus influenzae (physiology)
• Humans
• Magnetic Resonance Spectroscopy
• Male
• Mass Spectrometry
• Miller Fisher Syndrome (microbiology)
• Molecular Mimicry
• Molecular Sequence Data