Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/10427
Full metadata record
DC FieldValueLanguage
dc.contributor.authorMilland, Julieen
dc.contributor.authorYuriev, Elizabethen
dc.contributor.authorXing, Pei-Xiangen
dc.contributor.authorMcKenzie, Ian F Cen
dc.contributor.authorRamsland, Paul Aen
dc.contributor.authorSandrin, Mauro Sen
dc.date.accessioned2015-05-15T23:52:23Z
dc.date.available2015-05-15T23:52:23Z
dc.date.issued2007-08-28en
dc.identifier.citationImmunology and Cell Biology 2007; 85(8): 623-32en
dc.identifier.govdoc17724458en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/10427en
dc.description.abstractCarbohydrates are involved in many immunological responses including the rejection of incompatible blood, tissues and organs. Carbohydrate antigens with Galalpha(1,3)Gal epitopes are recognized by natural antibodies in humans and pose a major barrier for pig-to-human xenotransplantation. Genetically modified pigs have been established that have no functional alpha1,3-galactosyltransferase (alpha1,3GT), which transfers alphaGal to N-acetyllactosamine (LacNAc) type oligosaccharides. However, a low level of Galalpha(1,3)Gal is still expressed in alpha1,3GT knockout animals in the form of a lipid, isoglobotrihexosylceramide (iGb3), which is produced by iGb3 synthase on lactose (Lac) type core structures. Here, we define the reactivity of a series of monoclonal antibodies (mAb) generated in alpha1,3GT-/- mice immunized with rabbit red blood cells (RbRBC), as a rich source of lipid-linked antigens. Interestingly, one mAb (15.101) binds weakly to synthetic and cell surface-expressed Galalpha(1,3)Gal on LacNAc, but strongly to versions of the antigen on Lac cores, including iGb3. Three-dimensional models suggest that the terminal alpha-linked Gal binds tightly into the antibody-binding cavity. Furthermore, antibody interactions were predicted with the second and third monosaccharide units. Collectively, our findings suggest that although the terminal carbohydrate residues confer most of the binding affinity, the fine specificity is determined by subsequent residues in the oligosaccharide.en
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherAntibodies, Heterophile.immunologyen
dc.subject.otherAntibodies, Monoclonal.immunologyen
dc.subject.otherAntibody Affinityen
dc.subject.otherAntibody Specificity.immunologyen
dc.subject.otherAntigens.immunologyen
dc.subject.otherBinding Sites, Antibodyen
dc.subject.otherCarbohydrates.immunologyen
dc.subject.otherCell Lineen
dc.subject.otherDisaccharides.immunologyen
dc.subject.otherEnzyme-Linked Immunosorbent Assayen
dc.subject.otherEpitopes.immunologyen
dc.subject.otherGlycoconjugates.immunologyen
dc.subject.otherHumansen
dc.subject.otherHydrogen Bondingen
dc.subject.otherMiceen
dc.subject.otherModels, Molecularen
dc.subject.otherOligosaccharides.immunologyen
dc.titleCarbohydrate residues downstream of the terminal Galalpha(1,3)Gal epitope modulate the specificity of xenoreactive antibodies.en
dc.typeJournal Articleen
dc.identifier.journaltitleImmunology and cell biologyen
dc.identifier.affiliationDepartment of Surgery (Austin Health), University of Melbourne, Heidelberg, Victoria, Australia.en
dc.identifier.doi10.1038/sj.icb.7100111en
dc.description.pages623-32en
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/17724458en
Appears in Collections:Journal articles

Files in This Item:
There are no files associated with this item.


Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.