Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/10222
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dc.contributor.authorChristiansen, Daleen
dc.contributor.authorMouhtouris, Effieen
dc.contributor.authorMilland, Julieen
dc.contributor.authorZingoni, Alessandraen
dc.contributor.authorSantoni, Angelaen
dc.contributor.authorSandrin, Mauro Sen
dc.date.accessioned2015-05-15T23:36:13Z
dc.date.available2015-05-15T23:36:13Z
dc.date.issued2006-09-01en
dc.identifier.citationXenotransplantation; 13(5): 440-6en
dc.identifier.govdoc16925668en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/10222en
dc.description.abstractMany immunologically important interactions are mediated by leukocyte recognition of carbohydrates via cell surface receptors. Uncharacterized receptors on human natural killer (NK) cells interact with ligands containing the terminal Galalpha(1,3)Gal xenoepitope. The aim of this work was to isolate and characterize carbohydrate binding proteins from NK cells that bind alphaGal or other potential xenoepitopes, such as N-acetyllactosamine (NAcLac), created by the deletion of alpha1,3galactosyltransferase (GT) in animals.Initial analysis suggested the human C-type lectin NKRP1A bound to a pool of glycoconjugates, the majority of which contained the terminal Galalpha(1,3)Gal epitope. This was confirmed by high level binding of cells expressing NKRP1A to mouse laminin, which contains a large number of N-linked oligosaccharides with the Galalpha(1,3)Gal structure. The consequence of removing the terminal alphaGal was then investigated. Elevated NAcLac levels were observed on thymocytes from GT-/- mice. Exposing NAcLac on laminin, by alpha-galactosidase treatment, resulted in a significant increase in NKRP1A binding.NKRPIA binds to the alphaGal epitope. Moreover, exposing NAcLac by removal of alphaGal resulted in an increase in binding. This may be relevant in the later phases of xenotransplant rejection if GT-/- pigs, like GT-/- mice, display increased NAcLac expression.en
dc.language.isoenen
dc.subject.otherAmino Sugars.biosynthesis.immunologyen
dc.subject.otherAnimalsen
dc.subject.otherAntigen-Antibody Reactionsen
dc.subject.otherAntigens, Surface.immunologyen
dc.subject.otherCOS Cellsen
dc.subject.otherCercopithecus aethiopsen
dc.subject.otherDisaccharides.immunologyen
dc.subject.otherEpitopes.immunologyen
dc.subject.otherHumansen
dc.subject.otherLaminin.metabolismen
dc.subject.otherLectins, C-Type.immunologyen
dc.subject.otherMiceen
dc.subject.otherNK Cell Lectin-Like Receptor Subfamily Ben
dc.subject.otherTransplantation, Heterologous.immunologyen
dc.titleRecognition of a carbohydrate xenoepitope by human NKRP1A (CD161).en
dc.typeJournal Articleen
dc.identifier.journaltitleXenotransplantationen
dc.identifier.affiliationDepartment of Surgery, The University of Melbourne, Austin Health/Northern Health, Heidelberg, Victoria, Australiaen
dc.identifier.doi10.1111/j.1399-3089.2006.00332.xen
dc.description.pages440-6en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/16925668en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.languageiso639-1en-
item.fulltextNo Fulltext-
crisitem.author.deptInfectious Diseases-
crisitem.author.deptSurgery (University of Melbourne)-
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