Molecular arrangements in sphingolipids. The crystal structure of cerebroside

Pascher, I.; Sundell, Staffan

doi:10.1016/0009-3084(77)90033-0

Cited by 248 publications

(161 citation statements)

References 11 publications

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“…Conformers a,, b, and c correspond to the three minimum energy conformations for the saccharide-ceramide linkage as calculated by MM3. Furthermore, the conformations of a, and c agree with the crystal structures of cerebrosides (19,20). The preferred isoreceptor for the various adhesins is indicated in parentheses and the possible binding surfaces are indicated by colored lines.…”

Section: Figsupporting

confidence: 55%

“…Conformational calculations on globotriaosylceramide (GbO3) [Gal(al-4)LacCer], globotetraosylceramide (GbO4) [GalNAc(/31-3)Gal(al-4)LacCer], and globopentaosylceramide (GbO5) [GalNAc(al-3)GalNAc (f11-3)Gal(al-4)LacCer] were performed with the GESA program (15-17) and molecular mechanics (MM3) (18). The ceramide conformation was derived from the crystal structure of cerebrosides (19,20) and related membrane lipids (21). The conformation of the saccharide chains of GbO3, GbO4, and GbO5 was determined by HSEA calculations with the GESA program and by complementary MM3 calculations.…”

Section: Methodsmentioning

confidence: 99%

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Saccharide orientation at the cell surface affects glycolipid receptor function.

Strömberg

Nyholm

Pascher

et al. 1991

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

173

114

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Three allelic variants of P-pilus-associated G-adheslns (ectins) with different cell-binding properties were recently described. Here we have analyzed Eschenchia cofl HB101 strains expressing the recombinant G-adhesin variants for their ability to agglutinate erythrocytes from various species as this relates to the glycosphingolipid (GSL) MATERIALS AND METHODSBacteria, Growth Conditions, and Labeling. E. coli strain HB101 was used to express the P pilus-associated G-adhesins PapGJ96, PrsGJ96, and PapGAD1LO carried by the recombinant plasmids pPAP5, pPAP601, and pPIL110-35, respectively (10). Plasmid pPAP5 consists of the vector pBR322 and a 9.7-kilobase (kb) EcoRI/BamHI chromosomal fragment derived from E. coli J96 and encodes F13 P pili with the PapGJ96 adhesin (10). Plasmid pPAP601 is a pACYC184 derivative carrying another E. coli J96 chromosomal fragment encoding serologically identical F13 pili but having the PrsGJ% adhesin (10). Plasmid pPIL110-35 is a pACYC184 derivative containing a 16-kb EcoRI fragment of E. coli AD110 and encoding F72 P pili with the PapGAD110 adhesin (10).For the glycolipid binding assay, the bacteria were cultivated overnight at 37TC on Luria agar plates (10) supplemented with carbenicillin, chloramphenicol, and tetracycline (100, 20, and 10 jig/ml, respectively). Metabolically labeled bacteria were obtained by addition of [35S]methionine (600 Ci/mmol; 150-200 ,uCi per plate; 1 Ci = 37 GBq; Amersham). After growth, the bacteria were harvested by centrifugation, washed twice in phosphate-buffered saline (PBS) (pH 7.3), and resuspended in PBS.Hemagglutination Assay. For hemagglutination, 10 of fresh bacteria (109 cells per ml) and 10 of erythrocyte suspension (4%), both suspended in PBS at pH 7.3, were mixed on a glass slide. During gentle mixing for 5 min at room temperature, agglutination was visualized and scored (see Table 1).Erythrocyte Glycolipids. For the preparation of total acidic and neutral GSLs (10), fresh erythrocytes were washed twice in saline and 100 ml of erythrocyte concentrate was shaken continuously together with toluene and water (65 ml and 30 ml, respectively). After centrifugation (10,000 x g for 5 min), the purified membranes (10 g) at the toluene/water interface were extracted twice with methanol (100 ml), once with chloroform/methanol (2:1) (100 ml), and once with methanol (100 ml) for 25 min at 70TC. 9340The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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Section: Figsupporting

confidence: 55%

Section: Methodsmentioning

confidence: 99%

Saccharide orientation at the cell surface affects glycolipid receptor function.

Strömberg

Nyholm

Pascher

et al. 1991

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

173

114

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“…However, conformational analysis of hexosylceramides has shown a correlation between the ceramide structure and the orientation of the carbohydrate moiety. Thus, X-ray crystallography of galactosylceramide with sphingosine and 2-hydroxystearic acid demonstrated a shovel-like overall shape [24], whereas an NMR study of glucosylceramide with sphingosine and palmitic acid proposed a straighter conformation [25]. Furthermore, studies with anti-glycolipid antibodies and binding to intact cells [26] or well-defined liposomes [27] support the idea that the ceramide structure may direct the sugar head group conformation.…”

Section: Discussionmentioning

confidence: 99%

Studies on the binding of bacteria to glycolipids Two species of Propionibacterium apparently recognize separate epitopes on lactose of lactosylceramide

et al. 1988

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Two species of Propionibucterium were analysed regarding their binding to glycosphingolipids. Bacteria were labeled with rzsI and selective interaction with glycolipids on thin-layer chromatograms was revealed by autoradiography. The carbohydrate site in common for active molecular species appeared to be lactose. The two bacteria differed, however, in the overall binding pattern on the chromatogram, probably due to recognition of separate epitopes on lactose. P. freudenreichii bound only to lactosylceramide while P. granuloszon also recognized substituted lactosylceramide: Galal+ 3Gal/31 -r4Glc/7Cer, GlcNAcj?l-r3Ga431+4Glc&Cer and Gab?l~3GlcNAcj?l~3Gal/.?l+4Glc~er were active, but Galal +4Gal/?l -Xilcj?Cer was inactive. Also, there was an interesting dependence on ceramide structure in the case of lactosylceramide. P. freudenreichii bound to lactosylceramide with sphingosine and non-hydroxy fatty acids but not to species with sphingosine and 2-hydroxy fatty acids, phytosphingosine and non-hydroxy fatty acids or phytosphingosine and 2-hydroxy fatty acids. For P. grunufosum the situation was reversed. This may be explained by an inthtence of ceramide structure on the presentation of the two lactose epitopes at the assay surface. These results were supported by curves from the binding of labeled bacteria to glycolipids coated in microtiter wells and in part by binding to glycolipid-coated chicken erythrocytes.

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“…Therefore, hydroxyl groups in 2-hydroxy sphingolipids are likely to be important for the organization of PM microdomains in rice cells. Hydroxyl groups in sphingolipid fatty acids bind strongly to each other through hydrogen bonds (Pascher and Sundell, 1977;Löfgren and Pascher, 1977;Boggs et al, 1988), and hydroxyl groups are also largely present in LCBs of sphingolipids as (F) Quantification of ROS production in OsRbohB/H-KD suspension cells. Intensity of each well was measured by ImageJ software (http://rsbweb.nih.gov/ij/).…”

Section: Importance Of Pm Microdomain Organization By 2-hydroxy Sphinmentioning

confidence: 99%

“…Of the hundreds of sphingolipid species that exist in plants as a result of such modifications, many possess 2-hydroxy fatty acids (2-HFAs), containing a hydroxylated C-2 position (Markham et al, 2013) (Supplemental Figure 1A). 2-HFA contributes to the rigid binding of sphingolipids through hydrogen bonding between hydroxy groups in artificial membranes (Pascher and Sundell, 1977;Löfgren and Pascher, 1977), and sphingolipids containing 2-HFAs (2-hydroxy sphingolipids) reduce the lateral mobility of adipocyte membranes (Guo et al, 2010). Therefore, it is possible that 2-hydroxy sphingolipids contribute to the ordered structure of PM microdomains.…”

Section: Introductionmentioning

confidence: 99%

Plasma Membrane Microdomains Are Essential for Rac1-RbohB/H-Mediated Immunity in Rice

et al. 2016

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Numerous plant defense-related proteins are thought to congregate in plasma membrane microdomains, which consist mainly of sphingolipids and sterols. However, the extent to which microdomains contribute to defense responses in plants is unclear. To elucidate the relationship between microdomains and innate immunity in rice (Oryza sativa), we established lines in which the levels of sphingolipids containing 2-hydroxy fatty acids were decreased by knocking down two genes encoding fatty acid 2-hydroxylases (FAH1 and FAH2) and demonstrated that microdomains were less abundant in these lines. By testing these lines in a pathogen infection assay, we revealed that microdomains play an important role in the resistance to rice blast fungus infection. To illuminate the mechanism by which microdomains regulate immunity, we evaluated changes in protein composition, revealing that microdomains are required for the dynamics of the Rac/ROP small GTPase Rac1 and respiratory burst oxidase homologs (Rbohs) in response to chitin elicitor. Furthermore, FAHs are essential for the production of reactive oxygen species (ROS) after chitin treatment. Together with the observation that RbohB, a defense-related NADPH oxidase that interacts with Rac1, is localized in microdomains, our data indicate that microdomains are required for chitin-induced immunity through ROS signaling mediated by the Rac1-RbohB pathway.

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Molecular arrangements in sphingolipids. The crystal structure of cerebroside

Cited by 248 publications

References 11 publications

Saccharide orientation at the cell surface affects glycolipid receptor function.

Saccharide orientation at the cell surface affects glycolipid receptor function.

Studies on the binding of bacteria to glycolipids Two species of Propionibacterium apparently recognize separate epitopes on lactose of lactosylceramide

Plasma Membrane Microdomains Are Essential for Rac1-RbohB/H-Mediated Immunity in Rice

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