Anti-ganglioside complex antibodies associated with severe disability in GBS

Kaida, K.; Morita, Daiji; Kanzaki, Mami; Kamakura, Keiko; Motoyoshi, Kazuo; Hirakawa, Minako; Kusunoki, Susumu

doi:10.1016/j.jneuroim.2006.09.013

Cited by 98 publications

(76 citation statements)

References 20 publications

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“…In only one patient with CIDP and high titers of antibodies to GD1b and one with PN-IgM we found that testing for IgM antibodies to GSCs allowed to detect an additional intense IgM reactivity to the complexes formed by GM1 or GM2 with GT1b, as previously reported in a few patients with GBS and high anti-GD1b IgG (Kaida et al, 2008a), or by GM2 and GD1b, respectively, in the absence of reactivity to the individual gangliosides. No other patient showed new reactivities by this procedure indicating that, at odds with GBS and FS where approximately 5-10% of the patients were found to have antibody to GSCs in the absence of antibodies to individual gangliosides (Kaida et al, 2006(Kaida et al, , 2007(Kaida et al, , 2008b, this seldom occurred for IgM antibodies in patients with MMN or other chronic immune neuropathies.…”

Section: Discussionmentioning

confidence: 92%

“…At the same time in some patients the mixture of some gangliosides blocked the reactivity to the individual ganglioside forming the GSCs (negative interaction). In these patients reactivity to GSCs was variably related to some clinical features (Kaida et al, 2007(Kaida et al, , 2008a. Little is known on the presence of anti-GSCs IgM antibodies in MMN or other chronic immunemediated neuropathies.…”

Section: Introductionmentioning

confidence: 99%

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Anti-ganglioside complex IgM antibodies in multifocal motor neuropathy and chronic immune-mediated neuropathies

Nobile‐Orazio¹,

Giannotta²,

Briani³

2010

Journal of Neuroimmunology

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Section: Discussionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Anti-ganglioside complex IgM antibodies in multifocal motor neuropathy and chronic immune-mediated neuropathies

Nobile‐Orazio¹,

Giannotta²,

Briani³

2010

Journal of Neuroimmunology

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“…The major antibodies were identified as directed to GM1 (23). Antibodies causing more serious motor nerve paralysis were found to be directed to heterodimer structures, such as GD1a/GM1, GD1b/ GT1b, and GM1/GT1b, rather than single ganglioside structures (10,24).…”

Section: Discussionmentioning

confidence: 99%

Ganglioside GM2/GM3 complex affixed on silica nanospheres strongly inhibits cell motility through CD82/cMet-mediated pathway

Todeschini

Santos

Handa

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

115

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Ganglioside GM2 complexed with tetraspanin CD82 in glycosynaptic microdomain of HCV29 and other epithelial cells inhibits hepatocyte growth factor-induced cMet tyrosine kinase. In addition, adhesion of HCV29 cells to extracellular matrix proteins also activates cMet kinase through ''cross-talk '' of integrins with cMet, leading to inhibition of cell motility and growth. Present studies indicate that cell motility and growth are greatly influenced by expression of GM2, GM3, or GM2/GM3 complexes, which affect cMet kinase activity of various types of cells, based on the following series of observations: (i) Cells expressing CD82, cultured with GM2 and GM3 cocoated on silica nanospheres, displayed stronger and more consistent motility inhibition than those cultured with GM2 or GM3 alone or with other glycosphingolipids. (ii) GM2-GM3, in the presence of Ca 2؉ form a heterodimer, as evidenced by electrospray ionization (ESI) mass spectrometry and by specific reactivity with mAb 8E11, directed to GM2/GM3 dimer structure. (iii) Cells expressing cMet and CD82 were characterized by enhanced motility associated with HGF-induced cMet activation. Both cMet and motility were strongly inhibited by culturing cells with GM2/GM3 dimer coated on nanospheres. (iv) Adhesion of HCV29 or YTS-1/CD82 cells to laminin-5-coated plate activated cMet kinase in the absence of HGF, whereas GM2/GM3 dimer inhibited adhesioninduced cMet kinase activity and inhibited cell motility. (v) Inhibited cell motility as in i, iii, and iv was restored to normal level by addition of mAb 8E11, which blocks interaction of GM2/GM3 dimer with CD82. Signaling through Src and MAP kinases is activated or inhibited in close association with cMet kinase, in response to GM2/GM3 dimer interaction with CD82. Thus, a previously uncharacterized GM2/GM3 heterodimer complexed with CD82 inhibits cell motility through CD82-cMet or integrin-cMet pathway.glycosphingolipid ͉ growth factor receptor ͉ ldlD cells ͉ tyrosine kinase G lycosphingolipids (GSLs), including gangliosides, interact with specific membrane proteins, such as growth factor receptors, integrins, tetraspanins (TSPs), and nonreceptor cytoplasmic kinases (e.g., Src family kinases and small G proteins), to form glycosynaptic microdomains controlling GSL-dependent or -modulated cell adhesion, growth, and motility (for review, see refs. 1-3).Our previous studies indicate the following: (i) Ganglioside the GM3/TSP CD9 complex interacts with integrin ␣3␤1 or ␣5␤1 and inhibits motility of CD9-expressing tumor cells (4, 5). (ii) The GM3/CD9/CD81 complex inhibits tyrosine kinase associated with fibroblast growth factor receptor (FGFR) (6) and blocks functional interaction of integrins with FGFR (7). (iii) Enhancement of GM3 or CD9 level in bladder cancer cell line YTS-1 causes reversion to normal phenotype, whereby Src kinase activity is strongly inhibited (8).In contrast to these previous studies, focused on GM3-CD9 interaction that inhibits tumor cell motility, our recent studies (9) addressed the functional role of t...

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“…The clinical features of certain subtypes of GBS are composed of a myriad of pathologic subtypes, each of which is associated with specific antiganglioside antibodies; 20 thus, the inclusion of three single gangliosides – GM‐1, GM‐2, and GD1a – and the omission of others reduced the range of detection of antiganglioside antibodies associated with GBS. Furthermore, sera from GBS‐afflicted individuals react more readily to mixtures of gangliosides, known as ganglioside complexes, and not to their individual constituents 20 , 31 , 32 . In addition, this study and others 23 , 25 , 32 , 33 have utilized gangliosides of bovine brain origin for antibody detection in mouse and human sera with success.…”

Section: Discussionmentioning

confidence: 89%

“…To our knowledge, screening of antiganglioside antibodies has been performed only in persons presenting with clinical signs of GBS; therefore, the baseline levels of antiganglioside antibodies in the population remain unknown. Although antiganglioside antibodies involved with GBS cannot be treated as a definitive marker for the syndrome, they potentially play a key role in its pathophysiology, and their importance must not be underestimated 3 , 4 , 20 , 22 , 31 , 32 , 33 , 36 …”

Section: Discussionmentioning

confidence: 99%

No evidence of a link between influenza vaccines and Guillain–Barre syndrome–associated antiganglioside antibodies

Wang

Boltz

McElhaney

et al. 2011

Influenza Resp Viruses

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Please cite this paper as: Wang et al. (2011) No evidence of a link between influenza vaccines and Guillain–Barre syndrome–associated antiganglioside antibodies. Influenza and Other Respiratory Viruses 6(3), 159–166. Background Guillain–Barre syndrome (GBS) is a rare autoimmune disease characterized by acute, progressive peripheral neuropathy and is commonly associated with the presence of antiganglioside antibodies. Previously, influenza vaccination was linked with the increased incidence of GBS; however, whether antiganglioside antibodies are subsequently induced remains unresolved. Methods Sera from human subjects vaccinated with seasonal influenza vaccines from the 2007–2008, 2008–2009, or 1976–1977 influenza seasons were screened for the induction of immunity to influenza and the presence of antiganglioside antibodies pre‐ and post‐vaccination. Likewise, sera from mice vaccinated with seasonal influenza vaccines (1988–1989, 2007–2008) or “swine flu” pandemic vaccines (1976, 2009) were assessed in the same manner. Viruses were also screened for cross‐reacting ganglioside epitopes. Results Antiganglioside antibodies were found to recognize influenza viruses; this reactivity correlated with virus glycosylation. Antibodies to influenza viruses were detected in human and mouse sera, but the prevalence of antiganglioside antibodies was extremely low. Conclusions Although the correlation between antiganglioside antibody cross‐reactivity and glycosylation of viruses suggests the role of shared carbohydrate epitopes, no correlation was observed between hemagglutinin‐inhibition titers and the induction of antiganglioside antibodies after influenza vaccination.

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Anti-ganglioside complex antibodies associated with severe disability in GBS

Cited by 98 publications

References 20 publications

Anti-ganglioside complex IgM antibodies in multifocal motor neuropathy and chronic immune-mediated neuropathies

Anti-ganglioside complex IgM antibodies in multifocal motor neuropathy and chronic immune-mediated neuropathies

Ganglioside GM2/GM3 complex affixed on silica nanospheres strongly inhibits cell motility through CD82/cMet-mediated pathway

No evidence of a link between influenza vaccines and Guillain–Barre syndrome–associated antiganglioside antibodies

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