Ries, Annika

[["dc.bibliographiccitation.firstpage","3104"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Chemical Science"],["dc.bibliographiccitation.lastpage","3114"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Schütte, Ole Mathis"],["dc.contributor.author","Ries, Annika"],["dc.contributor.author","Orth, Alexander"],["dc.contributor.author","Patalag, Lukas J."],["dc.contributor.author","Römer, Winfried"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Werz, Daniel B."],["dc.date.accessioned","2017-09-07T11:46:54Z"],["dc.date.available","2017-09-07T11:46:54Z"],["dc.date.issued","2014"],["dc.description.abstract","The Shiga toxin B subunit (STxB), which is involved in cell membrane attachment and trafficking of Shiga holotoxin, binds specifically to the glycosphingolipid Gb(3). In biological membranes, Gb(3) glycosphingolipids differ in their fatty acid composition and there is strong evidence that the fatty acid alters the binding behaviour of STxB as well as the intracellular routing of the Shiga toxin/Gb(3) complex. To analyse the binding of STxB to different Gb(3)s, we chemically synthesized saturated, unsaturated, alpha-hydroxylated Gb(3)s and a combination thereof, all based on a C-24-fatty acid chain starting from monosaccharide building blocks, sphingosine and the respective fatty acids. These chemically well-defined Gb(3)s were inserted into solid supported phase-separated lipid bilayers composed of DOPC/sphingomyelin/cholesterol as a simple mimetic of the outer leaflet of animal cell membranes. By fluorescence- and atomic force microscopy the phase behaviour of the bilayer as well as the lateral organization of bound STxB were analysed. The fatty acid of Gb(3) significantly alters the ratio between the ordered and disordered phase and induces a third intermediate phase in the presence of unsaturated Gb(3). The lateral organization of STxB on the membranes varies significantly. While STxB attached to membranes with Gb(3)s with saturated fatty acids forms protein clusters, it is more homogeneously bound to membranes containing unsaturated Gb(3)s. Large interphase lipid redistribution is observed for alpha-hydroxylated Gb(3) doped membranes. Our results clearly demonstrate that the fatty acid of Gb(3) strongly influences the lateral organization of STxB on the membrane and impacts the overall membrane organization of phase-separated lipid membranes."],["dc.identifier.doi","10.1039/c4sc01290a"],["dc.identifier.gro","3142208"],["dc.identifier.isi","000338652900019"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10662"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5732"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","2041-6539"],["dc.relation.issn","2041-6520"],["dc.rights.access","openAccess"],["dc.title","Influence of Gb(3) glycosphingolipids differing in their fatty acid chain on the phase behaviour of solid supported membranes: chemical syntheses and impact of Shiga toxin binding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","15630"],["dc.bibliographiccitation.issue","28"],["dc.bibliographiccitation.journal","Physical Chemistry, Chemical Physics"],["dc.bibliographiccitation.lastpage","15638"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Bosse, Mathias"],["dc.contributor.author","Sibold, Jeremias"],["dc.contributor.author","Scheidt, Holger A."],["dc.contributor.author","Patalag, Lukas J."],["dc.contributor.author","Kettelhoit, Katharina"],["dc.contributor.author","Ries, Annika"],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Huster, Daniel"],["dc.date.accessioned","2020-12-10T18:11:27Z"],["dc.date.available","2020-12-10T18:11:27Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1039/C9CP02501D"],["dc.identifier.eissn","1463-9084"],["dc.identifier.issn","1463-9076"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16738"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74015"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Shiga toxin binding alters lipid packing and the domain structure of Gb 3 -containing membranes: a solid-state NMR study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","154907"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","The Journal of Chemical Physics"],["dc.bibliographiccitation.volume","142"],["dc.contributor.author","Yamamoto, Akihisa"],["dc.contributor.author","Abuillan, Wasim"],["dc.contributor.author","Burk, Alexandra S."],["dc.contributor.author","Koerner, Alexander"],["dc.contributor.author","Ries, Annika"],["dc.contributor.author","Werz, Daniel B."],["dc.contributor.author","Deme, Bruno"],["dc.contributor.author","Tanaka, Motomu"],["dc.date.accessioned","2018-11-07T09:58:24Z"],["dc.date.available","2018-11-07T09:58:24Z"],["dc.date.issued","2015"],["dc.description.abstract","The mechanical properties of multilayer stacks of Gb3 glycolipid that play key roles in metabolic disorders (Fabry disease) were determined quantitatively by using specular and off-specular neutron scattering. Because of the geometry of membrane stacks deposited on planar substrates, the scattered intensity profile was analyzed in a 2D reciprocal space map as a function of in-plane and out-of-plane scattering vector components. The two principal mechanical parameters of the membranes, namely, bending rigidity and compression modulus, can be quantified by full calculation of scattering functions with the aid of an effective cut-off radius that takes the finite sample size into consideration. The bulkier \"bent\" Gb3 trisaccharide group makes the membrane mechanics distinctly different from cylindrical disaccharide (lactose) head groups and shorter \"bent\" disaccharide (gentiobiose) head groups. The mechanical characterization of membranes enriched with complex glycolipids has high importance in understanding the mechanisms of diseases such as sphingolipidoses caused by the accumulation of non-degenerated glycosphingolipids in lysosomes or inhibition of protein synthesis triggered by the specific binding of Shiga toxin to Gb3. (C) 2015 Author(s)."],["dc.identifier.doi","10.1063/1.4918585"],["dc.identifier.isi","000353307700052"],["dc.identifier.pmid","25903910"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13807"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37356"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Inst Physics"],["dc.relation.issn","1089-7690"],["dc.relation.issn","0021-9606"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Influence of length and conformation of saccharide head groups on the mechanics of glycolipid membranes: Unraveled by off-specular neutron scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]