Gangliosides and allied glycosphingolipids in human peripheral nerve and spinal cord

Svennerholm, Lars; Boström, Kerstin; Fredman, Pam; Jungbjer, Birgitta; Lekman, Annika; Månsson, Jan‐Eric; Rynmark, Britt-Marie

doi:10.1016/0005-2760(94)90034-5

Cited by 177 publications

(104 citation statements)

References 38 publications

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“…GD3 is known to be located in human peripheral nerve and rat Schwann cell surface (Levison and McCarthy, 1989;Svennerholm et al, 1994). Goodyear et al (1999) showed that anti-GD3 mAbs were elicited from mice sensitized with LPS of C. jejuni from patients with Miller Fisher syndrome and that they possess a binding activity to the NMJ region of mice.…”

Section: Discussionmentioning

confidence: 99%

Molecular mimicry: Sensitization of Lewis rats with Campylobacter jejuni lipopolysaccharides induces formation of antibody toward GD3 ganglioside

Usuki

Thompson

Rivner

et al. 2005

J of Neuroscience Research

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Recently we have reported cases of demyelinating inflammatory neuropathy showing elevated titers of anti-GD3 antibodies, which occurs rarely in Guillain-Barré syndrome. To examine the correlation between the anti-GD3 antibody titer and Campylobacter jejuni infection, we sensitized female Lewis rats with lipopolysaccharides (LPSs) from serotype HS19 of C. jejuni and examined changes in nerve conduction velocity and nerve conduction block (P/D ratio). After 16 weeks of sensitization, animals revealed decreases of nerve conduction velocity and conduction block (P/D ratio) and high titer of anti-GD3 antibodies. These anti-GD3 antibodies also blocked transmission in neuromuscular junctions of spinal cord-muscle cells cocultures. The GD3 epitope was verified to be located on the Schwann cell surface and nodes of Ranvier in rat sciatic nerve. To determine the target epitope for GD3 antibodies in causing nerve dysfunction, the LPS fraction containing the GD3 epitope was purified from the total LPS by using an anti-GD3 monoclonal antibody-immobilized affinity column. Subsequently, chemical analysis of the oligosaccharide portion was performed and confirmed the presence of a GD3-like epitope as having the following tetrasaccharide structure: NeuAcα2-8NeuAc2-3Galβ1-4Hep. Our data thus support the possibility of a contribution of GD3 mimicry as a potential pathogenic mechanism of peripheral nerve dysfunction. Keywordsganglioside; Guillain-Barré; syndrome; anti-ganglioside antibody; GD3; Campylobacter jejuni; LPS Guillain-Barré syndrome (GBS) is an acute immune-mediated peripheral neuropathy consisting of acute inflammatory demyelinating polyneuropathy (AIDP), acute motor neuropathy (AMAN), and related disorders. Anti-GM1 antibodies are often detected in patients with AIDP and AMAN (Kornberg et al., 1994;Arasaki et al., 1998;Hiraga et al., 2005). Many investigators have reported the association between an antecedent Campylobacter jejuni (C. jejuni) infection and subsequent development of GBS. The lipopolysaccharides (LPSs) of a certain serotype of C. jejuni have been shown to possess carbohydrate epitopes similar to *Correspondence to: Dr. Robert K. Yu, Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, GA 30912-2697. ryu@mcg.edu. NIH Public Access NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript gangliosides, which may serve as the putative pathogenic triggers for subsequent GBS onset. Thus, these disorders may develop as a result of C. jejuni infection. In addition to anti-GQ1b Abs, anti-GD3 Abs have been detected in the Miller Fisher variant of GBS (Chiba et al., 1992;Carpo et al., 1998;Susuki et al., 2001;Willison and Yuki, 2002;Willison et al., 2004).Recently we have reported cases of AIDP and chronic inflammatory demyelinating polyneuropathy (CIDP) showing high elevations of anti-GD3 Abs, which rarely occurs in GBS (Usuki et al., 2005). The question then arises of the origin of the antiglycolipid (anti-GSL) Abs in GBS, in particular, the mechanism of el...

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Section: Discussionmentioning

confidence: 99%

Molecular mimicry: Sensitization of Lewis rats with Campylobacter jejuni lipopolysaccharides induces formation of antibody toward GD3 ganglioside

Usuki

Thompson

Rivner

et al. 2005

J of Neuroscience Research

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show abstract

“…Its function is not completely understood, but it is thought to play an important role in the attachment of tumor cells to extracellular matrix proteins [43]. GD2 expression in normal fetal and adult tissues is primarily restricted to the neurons, skin melanocytes and peripheral nerve fibers [44]. Due to its high and relatively tumor-specific expression, GD2 is an attractive target for tumor-specific antibody therapy.…”

Section: Gd2 and Anti-gd2 Antibody Immunotherapymentioning

confidence: 99%

Fenretinide sensitizes multidrug-resistant human neuroblastoma cells to antibody-independent and ch14.18-mediated NK cell cytotoxicity

et al. 2012

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“…22,23 Polysialylated complex gangliosides are more concentrated in the Recent studies have indicated that a proportion of patients with FS and AMAN form of GBS who were seronegative when tested against individual gangliosides in solid phase assays become seropositive when tested with mixture of two different gangliosides. These novel observations raise the possibility that number of seronegative patients in GBS, particularly AIDP variant, could decrease as sera from these patients are tested against mixture of gangliosides/glycolipids.…”

Section: Gangliosidesmentioning

confidence: 99%

Autoantobodies activate small GTPase RhoA to modulate neurite outgrowth

Sheikh

2011

Small GTPases

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Gangliosides and allied glycosphingolipids in human peripheral nerve and spinal cord

Cited by 177 publications

References 38 publications

Molecular mimicry: Sensitization of Lewis rats with Campylobacter jejuni lipopolysaccharides induces formation of antibody toward GD3 ganglioside

Molecular mimicry: Sensitization of Lewis rats with Campylobacter jejuni lipopolysaccharides induces formation of antibody toward GD3 ganglioside

Fenretinide sensitizes multidrug-resistant human neuroblastoma cells to antibody-independent and ch14.18-mediated NK cell cytotoxicity

Autoantobodies activate small GTPase RhoA to modulate neurite outgrowth

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