Susceptibility of ganglioside GM<sub>1</sub> to a new bacterial neuraminidase

Sugano, Kentaro; Saito, Masaki; Nagai, Yoshitaka

doi:10.1016/0014-5793(78)80246-4

Cited by 33 publications

(10 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although intact lysosomes hydrolyzed gangliosides rather efficiently (Table I), the partially purified intralysosomal sialidase failed to exhibit this activity even in the presence of deoxycholate or cholate [24]. We have already presented evidence that, in the lysosomes, the activities towards gangliosides and bovine submaxillary mucin are associated with the lysosomal membrane (Table 1).…”

Section: Substrate Specificity O J Intvalysosomal Sialidasementioning

confidence: 91%

Rat‐liver lysosomal sialidase

Miyagi

Tsuiki

1984

European Journal of Biochemistry

109

View full text Add to dashboard Cite

Purified liver lysosomes, prepared from rats previously injected with Triton WR-1339, exhibited sialidase activity towards sialyllactose, fetuin, submaxillary mucin (bovine) and gangliosides, and could be disrupted hypotonically with little loss in these activities. After centrifugation, the activities with sialyllactose and fetuin were largely recovered in the supernatant, demonstrating that they were originally in the intralysosomal space. The activities towards submaxillary mucin and gangliosides, on the other hand, remained in the pellet. In the supernatant, activity with fetuin or orosomucoid was markedly reduced by protease inhibitors, suggesting that proteolysis of these glycoproteins may be prerequisite to sialidase activity.The intralysosomal sialidase was solubilized from the mitochondrial-lysosomal fraction of rat liver and partially purified by Sephadex G-200, or Sephadex G-200 followed by CM-cellulose. The enzyme was maximally active at pH 4.7 with sialyllactose as substrate and had a minimum relative molecular mass of 60000 k 5000 by gel filtration; it hydrolyzed a variety of sialooligosaccharides, those containing (a2+ 3)sialyl linkages being better substrates than those with (a2+6)sialyl linkages. The enzyme failed to attack submaxillary mucin and gangliosides. It was also inactive towards fetuin, orosomucoid and transferrin but capable of hydrolyzing glycopeptides from pronase digest of fetuin.In contrast to the intralysosomal silaidase, the sialidase partially purified from rat liver cytosol by (NH,),SO, fractionation followed by chromatography on DEAE-cellulose and CM-cellulose hydrolyzed fetuin and orosomucoid to the extent about half that for sialyllactose. The enzyme was maximally active at pH 5.8 and had a relative molecular mass of approximately 60000. It also hydrolyzed gangliosides but not submaxillary mucin.

show abstract

Section: Substrate Specificity O J Intvalysosomal Sialidasementioning

confidence: 91%

Rat‐liver lysosomal sialidase

Miyagi

Tsuiki

1984

European Journal of Biochemistry

109

View full text Add to dashboard Cite

show abstract

“…If they are not, GSLs should accumulate on earth, but this is unlikely. However, there have been very few reports of metabolic degradation of GSLs by microbes (12,13,27). This paper provides the first report of metabolic degradation of ganglio-series GSLs that generates GlcCer by culture with a single strain of bacteria.…”

Section: Discussionmentioning

confidence: 88%

“…Some microbes produce GSL-degrading enzymes, including sialidases (neuraminidase), which acts on the sialic acid residues of gangliosides (27); an endoglycoceramidase, which hydrolyzes the linkage between the oligosaccharide and Cer of various GSLs, including gangliosides (13); and a sphingolipid ceramide N-deacylase (SCDase), which hydrolyzes the N-acyl linkage of Cer in various GSLs, as well as sphingomyelin, to produce free fatty acids and the corresponding lyso-GSLs (12). However, these microbes hydrolyze a specific linkage of gangliosides, resulting in incomplete degradation of the substrates.…”

mentioning

confidence: 99%

Utilization of Ganglioside-Degrading Paenibacillus sp. Strain TS12 for Production of Glucosylceramide

Sumida

Sueyoshi

Ito

2002

Appl Environ Microbiol

View full text Add to dashboard Cite

Gangliosides, sialic acid-containing glycosphingolipids, are membrane constituents of vertebrates and are known to have important roles in cellular differentiation, adhesion, and recognition. We report here the isolation of a bacterium capable of degrading gangliotetraose-series gangliosides and a new method for the production of glucosylceramide with this bacterium. GM1a ganglioside was found to be sequentially degraded by Paenibacillus sp. strain TS12, which was isolated from soil, as follows: GM1a 3 asialo GM1 3 asialo GM2 3 lactosylceramide 3 glucosylceramide. TS12 was found to produce a series of ganglioside-degrading enzymes, such as sialidases, ␤-galactosidases, and ␤-hexosaminidases. TS12 also produced ␤-glucosidases, but glucosylceramide was somewhat resistant to the bacterial enzyme under the conditions used. Taking advantage of the specificity, we developed a new method for the production of glucosylceramide using TS12 as a biocatalyst. The method involves the conversion of crude bovine brain gangliosides to glucosylceramide by coculture with TS12 and purification of the product by chromatography with Wakogel C-300 HG.

show abstract

“…It must be emphasized that these latter enzymes have a specific action on GM1 ganglioside (detected. in LLC-MK2 cells by thin-layer chromatography; data not shown) which is believed to be resistant to various neuraminidases of viral, bacterial and mammalian origin (Sugano et al, 1978;Suzuki et al, 1980). The role of GMI in SA-11 binding to LLC-MK2 cells was investigated (i) by incubating MBPG or different, purified gangliosides isolated from MBPG with the virus and measuring their effect on virus infection, (ii) by measuring the effect of MBPG and GM1 on virus binding, (iii) by coating C. perfringens neuraminidase-treated cells with MBPG or GM1 and determining whether they recover susceptibility to SA-11 infection and (iv) by evaluating the specific binding of SA-11 to MBPG and GM 1 attached to a plastic surface.…”

Section: Discussionmentioning

confidence: 98%

“…Both neuraminidases from V. cholerae and influenza virus hydrolyse ~,2-6' and ~t,2-3' ketosidic linkages (Gottschalk & Drzeniek, 1972); neuraminidase from C. perfringens hydrolyses GM 1 and GM2 gangliosides when these glycolipids are monomeric, whereas this action is sterically hindered when gangliosides are aggregated (Rauvala, 1979); neuraminidase from A. ureafaciens hydrolyses ~,2-3', c~,2-6' and ~,2-8' linkages of NANA residues with a highly specific action on ganglioside GM1 (Sugano et al, 1978).…”

Section: Discussionmentioning

confidence: 99%

Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells

Superti

Donelli

1991

Journal of General Virology

View full text Add to dashboard Cite

The chemical nature of receptors involved in the attachment of simian rotavirus (SA-11) to a monkey kidney cell line (LLC-MK2) was investigated. Enzymic treatment of cells before virus infection indicated that membrane proteins and phospholipids are not involved in virus attachment, whereas sialic acid and galactose participate in the receptor structure to differing extents. Incubation ofSA-11 with bovine brain gangliosides before infection strongly reduced its ability to bind to cell membranes. Similar experiments with individual purified gangliosides from bovine brain showed that virus infection was prevented by preincubation with GM1. Moreover, desialylated cells regained susceptibility to virus infection when coated with whole gangliosides or GM1 immediately after Clostridium perfringens neuraminidase treatment. The binding of SA-11 to whole gangliosides or GM1 was quantified by an ELISA procedure. The results suggest that gangliosides, mainly GM 1, are part of the receptor structure for SA-I 1 of susceptible LLC-MK2 cells.

show abstract

Susceptibility of ganglioside GM₁ to a new bacterial neuraminidase

Cited by 33 publications

References 13 publications

Rat‐liver lysosomal sialidase

Rat‐liver lysosomal sialidase

Utilization of Ganglioside-Degrading Paenibacillus sp. Strain TS12 for Production of Glucosylceramide

Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells

Contact Info

Product

Resources

About

Susceptibility of ganglioside GM1 to a new bacterial neuraminidase

Cited by 33 publications

References 13 publications

Rat‐liver lysosomal sialidase

Rat‐liver lysosomal sialidase

Utilization of Ganglioside-Degrading Paenibacillus sp. Strain TS12 for Production of Glucosylceramide

Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells

Contact Info

Product

Resources

About

Susceptibility of ganglioside GM₁ to a new bacterial neuraminidase