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Rati Choksi - One of the best experts on this subject based on the ideXlab platform.
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motor neuropathies and serum igm binding to ns6s heparin disaccharide or GM1 ganglioside
Journal of Neurology Neurosurgery and Psychiatry, 2010Co-Authors: Alan Pestronk, Miguel Chuquilin, Rati ChoksiAbstract:Background Serum IgM binding to GM1 ganglioside (GM1) is often associated with chronic acquired motor neuropathies. This study compared the frequency and clinical associations of serum IgM binding to a different antigen, a disulphated heparin disaccharide (NS6S), with results of IgM binding to GM1. Methods Serums and clinical features were retrospectively compared from 75 patients with motor neuropathies and 134 controls with amyotrophic lateral sclerosis (ALS), chronic immune demyelinating polyneuropathy (CIDP) and sensory neuropathies. Clinical correlations of positive IgM anti-GM1 testing found in 27 of 2113 unselected serums were also reviewed. Serum testing for IgM binding to NS6S and GM1 used covalent antigen linkage to ELISA plates. Results High titre IgM binding to NS6S and GM1 each occurred in 43%, and to one of the two in 64%, of motor neuropathy patients. Motor neuropathy syndromes were present in 25 of 27 patients with high titre serum IgM binding to GM1 in the unselected serums. IgM anti-GM1 or NS6S antibody related motor neuropathy syndromes usually have asymmetric, predominantly distal, upper extremity weakness. Conclusions IgM binding to NS6S disaccharide is associated with motor neuropathy syndromes and occurs with similar frequency to IgM binding to GM1. Testing for IgM binding to NS6S in addition to GM1 increases the frequency of finding IgM autoantibodies in motor neuropathies from 43% to 64%. High titres of serum IgM binding to GM1, tested with covalent ELISA methodology, have 93% specificity for motor neuropathy syndromes. High titres of serum IgM binding to NS6S have specificity for immune motor neuropathies compared with ALS and CIDP.
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multifocal motor neuropathy serum igm anti GM1 ganglioside antibodies in most patients detected using covalent linkage of GM1 to elisa plates
Neurology, 1997Co-Authors: Alan Pestronk, Rati ChoksiAbstract:IgM anti-GM1 antibodies occur with increased frequency in the serum of patients with multifocal motor neuropathy (MMN). We tested the ability of serum IgM from patients with MMN to bind to GM1 ganglioside covalently bound to secondary amino groups on ELISA plates (Co-GM1). The Co-GM1 technique detected high titer (>1,800), selective, serum IgM binding to GM1 ganglioside in 85% of our MMN patients (23/27), a significantly greater frequency compared with figures of 37% and 52% found using our previous testing methods. Selective IgM anti-GM1 antibodies showed disease specificity. The only other patients with selective, high-titer IgM anti-GM1 antibodies had either chronic motor neuropathy without conduction block or acute immune neuropathy in China. No patient from the amyotrophic lateral sclerosis, chronic inflammatory demyelinating polyneuropathy, Guillain-Barre, or systemic immune disorder control groups had selective IgM anti-GM1 antibodies at titers greater than 1,800 detected using Co-GM1 ganglioside as ELISA antigen. Titers of IgM anti-GM1 antibodies in MMN(averaging 31,000 ± 15,000) were more than fourfold higher with Co-GM1 than with previous anti-GM1 assay methods, using conventional ELISA plates with GM-1 antigen alone (7,200 ± 4,400) or in a lipid environment(3,600 ± 1,300). We conclude that using ELISA testing with Co-GM1 antigen, serum anti-GM1 autoantibodies are a useful marker for MMN, because they are present in 85% of MMN patients and, at titers greater than 1,800, have strong specificity for immune-mediated motor neuropathies.
Rumiana Dimova - One of the best experts on this subject based on the ideXlab platform.
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the glycolipid GM1 reshapes asymmetric biomembranes and giant vesicles by curvature generation
Proceedings of the National Academy of Sciences of the United States of America, 2018Co-Authors: Raktim Dasgupta, Markus S Miettinen, Nico Fricke, Reinhard Lipowsky, Rumiana DimovaAbstract:The ganglioside GM1 is present in neuronal membranes at elevated concentrations with an asymmetric spatial distribution. It is known to generate curvature and can be expected to strongly influence the neuron morphology. To elucidate these effects, we prepared giant vesicles with GM1 predominantly present in one leaflet of the membrane, mimicking the asymmetric GM1 distribution in neuronal membranes. Based on pulling inward and outward tubes, we developed a technique that allowed the direct measurement of the membrane spontaneous curvature. Using vesicle electroporation and fluorescence intensity analysis, we were able to quantify the GM1 asymmetry across the membrane and to subsequently estimate the local curvature generated by the molecule in the bilayer. Molecular-dynamics simulations confirm the experimentally determined dependence of the membrane spontaneous curvature as a function of GM1 asymmetry. GM1 plays a crucial role in connection with receptor proteins. Our results on curvature generation of GM1 point to an additional important role of this ganglioside, namely in shaping neuronal membranes.
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GM1 softens the membrane induces domains and causes spontaneous tubulation in giant vesicles
Biophysical Journal, 2017Co-Authors: Rumiana Dimova, Raktim Dasgupta, Nico Fricke, Tripta Bhatia, Jaime Agudocanalejo, Reinhard LipowskyAbstract:The ganglioside GM1 is present in neuronal membranes at elevated concentrations with an asymmetric spatial distribution. It is known to generate curvature and can be expected to strongly influence the neuron morphology. To elucidate these effects, we incorporated GM1 into giant unilamellar vesicles (GUVs) made of POPC. We found that even a few mol% of GM1 soften the fluid bilayer significantly as measured using fluctuation analysis, vesicle electrodeformation and micropipette aspiration. At room temperature and for GM1 fractions at and above ∼5 mol%, we detect the formation of GM1-rich gel-like domains. We use fluorescence microscopy to build a partial phase diagram of the binary mixture (Fricke and Dimova, Biophys. J. 2016, in press). After diluting the vesicle suspension with the native buffer, we observe spontaneous formation of nanotubes suggesting desorption of GM1 from the outer membrane leaflet and generation of spontaneous curvature stabilizing the tubes. Employing electroporation of GUVs, we assess the GM1 asymmetry. The associated spontaneous curvature is measured using two approaches: micropipette aspiration of GUVs and pulling of inward and outward membrane tubes via bead manipulation with optical tweezers (Dasgupta and Dimova, J. Phys. D. Appl. Phys. 47:282001, 2014). GM1 plays a crucial role in connection with receptor proteins. However, our results that GM1 decreases bending rigidity, causes spontaneous curvature and induces phase separation in the membrane point to an additional important role of this ganglioside, namely shaping neuronal membranes. This work is part of the MaxSynBio consortium, which is jointly funded by the Federal Ministry of Education and Research of Germany and the Max Planck Society.
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GM1 softens popc membranes and induces the formation of micron sized domains
Biophysical Journal, 2016Co-Authors: Nico Fricke, Rumiana DimovaAbstract:Abstract The influence of the glycolipid GM1 on the physical properties of POPC membranes was studied systematically by using different methods applied to giant and large unilamellar vesicles. The charge per GM1 molecule in the membrane was estimated from electrophoretic mobility measurements. Optical microscopy and differential scanning calorimetry were employed to construct a partial phase diagram of the GM1/POPC system. At room temperature, phase separation in the membrane was detected for GM1 fractions at and above ∼5 mol %, whereby GM1-rich gel-like domains were observed by fluorescent microscopy. Fluctuation analysis, vesicle electrodeformation, and micropipette aspiration were used to assess the bending rigidity of the membrane as a function of GM1 content. In the fluid phase, GM1 was shown to strongly soften the bilayer. In the region of coexistence of fluid and gel-like domains, the micropipette aspiration technique allowed measurements of the bending rigidity of the fluid phase only, whereas electrodeformation and fluctuation analysis were affected by the presence of the gel-phase domains. The observation that GM1 decreased the bilayer bending rigidity is important for understanding the role of this ganglioside in the flexibility of neuronal membranes.
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Measuring the Intrinsic Curvature of Ganglioside GM1
Biophysical Journal, 2015Co-Authors: Raktim Dasgupta, Reinhard Lipowsky, Rumiana DimovaAbstract:The ganglioside GM1, which is present at elevated concentrations in neuron cells and is distributed asymmetrically across their membrane, is known to generate curvature and can be expected to strongly influence the neuron morphology. To elucidate these curvature effects of GM1, one would like to study appropriate model systems but the development of such systems faces several difficulties. First, mimicking the asymmetric distribution of GM1 across the cell membrane in model membranes poses a major challenge. Second, commonly used methods based on fluorescence microscopy for investigating membrane curvature modulation by proteins/lipids cannot be directly applied to GM1 because that requires GM1 molecules are labeled or complexed with suitable fluorophores. But the spontaneous curvatures of these fluorescently labeled analogs are significantly different from that of the label free GM1. Here we report the results of our investigations on measuring the intrinsic curvature of GM1 molecules. We could successfully prepare giant unilamellar vesicles from lipid mixture having 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine and varying fractions of GM1. GM1 was predominantly present at the inner leaflet. A technique was developed to pull inward nanotubes in the vesicle (Dasgupta & Dimova, J. Phys. D Appl. Phys. 47:282001, 2014), where an optically trapped latex bead was first manipulated across the lipid membrane into the vesicle interior and then used as a handle for pulling an in-tube. The force transducer property of the optical trap allowed measuring the tube pulling force with high precision. By studying the tube pulling force as a function of membrane tension imposed by an aspiration micropipette, we could estimate that the mean curvature locally induced by single GM1 molecules is ∼1/(4.78±0.29nm).
Young-kug Choo - One of the best experts on this subject based on the ideXlab platform.
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ganglioside GM1 influences the proliferation rate of mouse induced pluripotent stem cells
Journal of Biochemistry and Molecular Biology, 2012Co-Authors: Kyutae Chang, Yoonju Na, Gislain Moussavou, Kinarm Ko, Kisung Ko, Kyunga Hwang, Eunjeong Jeong, Young-kug ChooAbstract:Gangliosides play important roles in the control of several biological processes, including proliferation and transmembrane signaling. In this study, we demonstrate the effect of ganglioside GM1 on the proliferation of mouse induced pluripotent stem cells (miPSCs). The proliferation rate of miPSCs was lower than in mouse embryonic stem cells (mESCs). Fluorescence activated cell sorting analysis showed that the percentage of cells in the G2/M phase in miPSCs was lower than that in mESCs. GM1 was expressed in mESCs, but not miPSCs. To confirm the role of GM1 in miPSC proliferation, miPSCs were treated with GM1. GM1-treated miPSCs exhibited increased cell proliferation and a larger number of cells in the G2/M phase. Furthermore, phosphorylation of mitogen-activated protein kinases was increased in GM1-treated miPSCs. [BMB Reports 2012; 45(12): 713-718]
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Distribution of gangliosides, GM1 and GM3, in the rat oviduct.
Molecules and Cells, 1999Co-Authors: Young-kug ChooAbstract:: It is known that gangliosides, being ubiquitous membrane components, play important roles in cell-cell recognition, differentiation and transmembrane signalling. GM3, GM1 and GD1a were detected in the rat oviduct as major gangliosides by thin-layer chromatography (TLC) analysis. The total amounts of gangliosides from the oviducts at various times after hormone injection were not much changed. In order to identify their distribution and possible changes during ovulation, frozen sections of the rat oviducts were stained with specific monoclonal antibodies (MAbs) against the ganglio-series gangliosides. GM3 and GM1 were expressed in a different manner, but GD1a and other gangliosides were not immunohistochemically detected. In the ampullar region, GM3 was expressed in all the stroma and epithelial cells, but not GM1. GM1 was also not observed in epithelial cells. Staining by anti-GM1 monoclonal antibodies revealed long and minute thread-like structures in some of the stroma cells, whereas anti-GM3 monoclonal antibodies stained the entire cytoplasm, but not the nucleus, of all the stroma and epithelial cells. Other ganglio-series gangliosides, including GD1a, were not detected to some extent in the ampullar region by immunohistochemistry. Thus, these data suggest that GM3 and GM1 are oviduct-specific gangliosides.
Thomas N. Seyfried - One of the best experts on this subject based on the ideXlab platform.
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myelin abnormalities in the optic and sciatic nerves in mice with GM1 gangliosidosis
Asn Neuro, 2015Co-Authors: Karie A Heinecke, Alessandra Dazzo, Adrienne M Luoma, Daniel A Kirschner, Thomas N. SeyfriedAbstract:GM1-gangliosidosis is a glycosphingolipid lysosomal storage disease involving accumulation of GM1 and its asialo form (GA1) primarily in the brain. Thin-layer chromatography and X-ray diffraction were used to analyze the lipid content/composition and the myelin structure of the optic and sciatic nerves from 7- and 10-month old β-galactosidase (β-gal) +/? and β-gal −/− mice, a model of GM1gangliosidosis. Optic nerve weight was lower in the β-gal −/− mice than in unaffected β-gal +/? mice, but no difference was seen in sciatic nerve weight. The levels of GM1 and GA1 were significantly increased in both the optic nerve and sciatic nerve of the β-gal −/− mice. The content of myelin-enriched cerebrosides, sulfatides, and plasmalogen ethanolamines was significantly lower in optic nerve of β-gal −/− mice than in β-gal +/? mice; however, cholesteryl esters were enriched in the β-gal −/− mice. No major abnormalities in these lipids were detected in the sciatic nerve of the β-gal −/− mice. The abnormalities in GM1 ...
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Filipin recognizes both GM1 and cholesterol in GM1 gangliosidosis mouse brain
Journal of Lipid Research, 2011Co-Authors: Julian R. Arthur, Karie A Heinecke, Thomas N. SeyfriedAbstract:Filipin is an antibiotic polyene widely used as a histochemical marker for cholesterol. We previously reported cholesterol/fi lipin-positive staining in brain of -galactosidase ( -gal) knockout ( / ) mice (GM1 gangli- osidosis). The content and distribution of cholesterol and gangliosides was analyzed in plasma membrane (PM) and microsomal (MS) fractions from whole-brain tissue of 15 week-old control ( -gal +/ ) and GM1 gangliosidosis ( -gal / ) mice. Total ganglioside content ( g sialic acid/ mg protein) was 3-fold and 7-fold greater in the PM and MS fractions, respectively, in gal / mice than in gal +/ mice. GM1 content was 30-fold and 50-fold greater in the PM and MS fractions, respectively. In contrast, unesterifi ed cholesterol content ( g/mg protein) was similar in the PM and the MS fractions of the gal / and gal +/ mice. Filipin is known to bind to various sterol derivatives and phospholipids on thin-layer chromatograms. Biochemical evidence is presented showing that fi lipin also binds to GM1 with an affi nity similar to that for cholesterol, with a corre- sponding fl uorescent reaction. Our data suggest that the GM1 storage seen in the -gal / mouse contributes to the fi lipin ultraviolet fl uorescence observed in GM1 gangli- osidosis brain. The data indicate that in addition to choles- terol, fi lipin can also be useful for detecting GM1. —Arthur, J. R., K. A. Heinecke, and T. N. Seyfried. Filipin recognizes both GM1 and cholesterol in GM1 gangliosidosis mouse brain. J. Lipid Res . 2011. 52: 1345-1351.
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AAV-mediated gene delivery in adult GM1-gangliosidosis mice corrects lysosomal storage in CNS and improves survival
PLoS ONE, 2010Co-Authors: Rena C. Baek, Marike L.d. Boekman, Stanley G. Leroy, Laryssa A. Tierney, Thomas N. Seyfried, Alessandra D'azzo, Michael A Sandberg, Miguel Sena-estevesAbstract:Background: GM1-gangliosidosis is a glycosphingolipid (GSL) lysosomal storage disease caused by a genetic deficiency of acid b-galactosidase (bgal), which results in the accumulation of GM1-ganglioside and its asialo-form (GA1) primarily in the CNS. Age of onset ranges from infancy to adulthood, and excessive ganglioside accumulation produces progressive neurodegeneration and psychomotor retardation in humans. Currently, there are no effective therapies for the treatment of GM1-gangliosidosis. Methodology/PrincipalFindings: In this study we examined the effect of thalamic infusion of AAV2/1-bgal vector in adult GM1 mice on enzyme distribution, activity, and GSL content in the CNS, motor behavior, and survival. Six to eight week-old GM1 mice received bilateral injections of AAV vector in the thalamus, or thalamus and deep cerebellar nuclei (DCN) with pre-determined endpoints at 1 and 4 months post-injection, and the humane endpoint, or 52 weeks of age. Enzyme activity was elevated throughout the CNS of AAV-treated GM1 mice and GSL storage nearly normalized in most structures analyzed, except in the spinal cord which showed ,50% reduction compared to age-matched untreated GM1 mice spinal cord. Survival was significantly longer in AAV-treated GM1 mice (52 wks) than in untreated mice. However the motor performance of AAV-treated GM1 mice declined over time at a rate similar to that observed in untreated GM1 mice. Conclusions/Significance: Our studies show that the AAV-modified thalamus can be used as a ‘built-in’ central node network for widespread distribution of lysosomal enzymes in the mouse cerebrum. In addition, this study indicates that thalamic delivery of AAV vectors should be combined with additional targets to supply the cerebellum and spinal cord with therapeutic levels of enzyme necessary to achieve complete correction of the neurological phenotype in GM1 mice.
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complete correction of enzymatic deficiency and neurochemistry in the GM1 gangliosidosis mouse brain by neonatal adeno associated virus mediated gene delivery
Molecular Therapy, 2007Co-Authors: Rena C. Baek, Thomas N. Seyfried, Marike L D Broekman, Laryssa A Comer, Juliet L Fernandez, Miguel SenaestevesAbstract:GM1-gangliosidosis is a glycosphingolipid (GSL) lysosomal storage disease caused by autosomal recessive deficiency of lysosomal acid β-galactosidase (βgal), and characterized by accumulation of GM1-ganglioside and GA1 in the brain. Here we examined the effect of neonatal intracerebroventricular (i.c.v.) injection of an adeno-associated virus (AAV) vector encoding mouse βgal on enzyme activity and brain GSL content in GM1-gangliosidosis (βgal−/−) mice. Histological analysis of βgal distribution in 3-month-old AAV-treated βgal−/− mice showed that enzyme was present at high levels throughout the brain. Biochemical quantification showed that βgal activity in AAV-treated brains was 7- to 65-fold higher than in wild-type controls and that brain GSL levels were normalized. Cerebrosides and sulfatides, which were reduced in untreated βgal−/− mice, were restored to normal levels by AAV treatment. In untreated βgal−/− brains, cholesterol was present at normal levels but showed abnormal cellular distribution consistent with endosomal/lysosomal localization. This feature was also corrected in AAV-treated mice. The biochemical and histological parameters analyzed in this study showed that normal brain neurochemistry was achieved in AAV-treated βgal−/− mice. Therefore we show for the first time that neonatal AAV-mediated gene delivery of lysosomal βgal to the brain may be an effective approach for treatment of GM1-gangliosidosis.
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substrate reduction reduces gangliosides in postnatal cerebrum brainstem and cerebellum in GM1 gangliosidosis mice
Journal of Lipid Research, 2005Co-Authors: Julie L. Kasperzyk, Alessandra Dazzo, Frances M. Platt, Joseph Alroy, Thomas N. SeyfriedAbstract:II3NeuAc-GgOse4Cer (GM1) gangliosidosis is an incurable lysosomal storage disease caused by a deficiency in acid beta-galactosidase (beta-gal), resulting in the accumulation of ganglioside GM1 and its asialo derivative GgOse4Cer (GA1) in the central nervous system, primarily in the brain. In this study, we investigated the effects of N-butyldeoxygalacto-nojirimycin (N B-DGJ), an imino sugar that inhibits ganglioside biosynthesis, in normal C57BL/6J mice and in beta-gal knockout (beta-gal-/-) mice from postnatal day 9 (p-9) to p-15. This is a period of active cerebellar development and central nervous system (CNS) myelinogenesis in the mouse and would be comparable to late-stage embryonic and early neonatal development in humans. N B-DGJ significantly reduced total ganglioside and GM1 content in cerebrum-brainstem (C-BS) and in cerebellum of normal and beta-gal-/- mice. N B-DGJ had no adverse effects on body weight or C-BS/cerebellar weight, water content, or thickness of the external cerebellar granule cell layer. Sphingomyelin was increased in C-BS and cerebellum, but no changes were found for cerebroside (a myelin-enriched glycosphingolipid), neutral phospholipids, or GA1 in the treated mice. Our findings indicate that the effects of N B-DGJ in the postnatal CNS are largely specific to gangliosides and suggest that N B-DGJ may be an effective early intervention therapy for GM1 gangliosidosis and other ganglioside storage disorders.
Alan Pestronk - One of the best experts on this subject based on the ideXlab platform.
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motor neuropathies and serum igm binding to ns6s heparin disaccharide or GM1 ganglioside
Journal of Neurology Neurosurgery and Psychiatry, 2010Co-Authors: Alan Pestronk, Miguel Chuquilin, Rati ChoksiAbstract:Background Serum IgM binding to GM1 ganglioside (GM1) is often associated with chronic acquired motor neuropathies. This study compared the frequency and clinical associations of serum IgM binding to a different antigen, a disulphated heparin disaccharide (NS6S), with results of IgM binding to GM1. Methods Serums and clinical features were retrospectively compared from 75 patients with motor neuropathies and 134 controls with amyotrophic lateral sclerosis (ALS), chronic immune demyelinating polyneuropathy (CIDP) and sensory neuropathies. Clinical correlations of positive IgM anti-GM1 testing found in 27 of 2113 unselected serums were also reviewed. Serum testing for IgM binding to NS6S and GM1 used covalent antigen linkage to ELISA plates. Results High titre IgM binding to NS6S and GM1 each occurred in 43%, and to one of the two in 64%, of motor neuropathy patients. Motor neuropathy syndromes were present in 25 of 27 patients with high titre serum IgM binding to GM1 in the unselected serums. IgM anti-GM1 or NS6S antibody related motor neuropathy syndromes usually have asymmetric, predominantly distal, upper extremity weakness. Conclusions IgM binding to NS6S disaccharide is associated with motor neuropathy syndromes and occurs with similar frequency to IgM binding to GM1. Testing for IgM binding to NS6S in addition to GM1 increases the frequency of finding IgM autoantibodies in motor neuropathies from 43% to 64%. High titres of serum IgM binding to GM1, tested with covalent ELISA methodology, have 93% specificity for motor neuropathy syndromes. High titres of serum IgM binding to NS6S have specificity for immune motor neuropathies compared with ALS and CIDP.
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multifocal motor neuropathy serum igm anti GM1 ganglioside antibodies in most patients detected using covalent linkage of GM1 to elisa plates
Neurology, 1997Co-Authors: Alan Pestronk, Rati ChoksiAbstract:IgM anti-GM1 antibodies occur with increased frequency in the serum of patients with multifocal motor neuropathy (MMN). We tested the ability of serum IgM from patients with MMN to bind to GM1 ganglioside covalently bound to secondary amino groups on ELISA plates (Co-GM1). The Co-GM1 technique detected high titer (>1,800), selective, serum IgM binding to GM1 ganglioside in 85% of our MMN patients (23/27), a significantly greater frequency compared with figures of 37% and 52% found using our previous testing methods. Selective IgM anti-GM1 antibodies showed disease specificity. The only other patients with selective, high-titer IgM anti-GM1 antibodies had either chronic motor neuropathy without conduction block or acute immune neuropathy in China. No patient from the amyotrophic lateral sclerosis, chronic inflammatory demyelinating polyneuropathy, Guillain-Barre, or systemic immune disorder control groups had selective IgM anti-GM1 antibodies at titers greater than 1,800 detected using Co-GM1 ganglioside as ELISA antigen. Titers of IgM anti-GM1 antibodies in MMN(averaging 31,000 ± 15,000) were more than fourfold higher with Co-GM1 than with previous anti-GM1 assay methods, using conventional ELISA plates with GM-1 antigen alone (7,200 ± 4,400) or in a lipid environment(3,600 ± 1,300). We conclude that using ELISA testing with Co-GM1 antigen, serum anti-GM1 autoantibodies are a useful marker for MMN, because they are present in 85% of MMN patients and, at titers greater than 1,800, have strong specificity for immune-mediated motor neuropathies.
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Autoantibodies to GM1 ganglioside: different reactivity to GM1-liposomes in amyotrophic lateral sclerosis and lower motor neuron disorders.
Journal of the Neurological Sciences, 1991Co-Authors: Fang Li, Alan PestronkAbstract:Abstract We studied the ability of anti-GM1 ganglioside antibodies to bind to GM1 in a lipid, “membrane-like” environment. Liposomes containing GM1 were synthesized to simulate this environment. We then compared the binding of anti-GM1 a autoantibodies to GM1-liposomes and to purified GM1. Antibody binding was quantified using enzyme-linked immunosorbent assay methodology. Our results showed a 250-fold variation in the ability of anti-GM1 antibodies to bind to GM1-liposomes. There was no correlation between GM1-liposome binding and the carbohydrate specificities of the anti-GM1 antibodies. However, anti-GM1 antibodies from patients with amyotophic lateral sclerosis (ALS) showed a 4 fold greater binding to GM1-liposomes than antibodies from patients with lower motor neuron (LMN) syndromes. We conclude that a lipid, presumably “membrane-like”, environment may greatly influence the degree of anti-GM1 antibody binding to GM1. The low levels of anti-GM1 antibody binding to GM1-liposomes in patients with LMN syndromes may provide a diagnostic means for distinguishing these patients from those with ALS. Anti-GM1 antibodies from patients with ALS may bind especially well to neuronal membranes containing GM1 in vivo.