{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T07:47:26Z","timestamp":1792741646754,"version":"4.5.0"},"reference-count":131,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2005,10,21]],"date-time":"2005-10-21T00:00:00Z","timestamp":1129852800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Immunol Cell Biol"],"published-print":{"date-parts":[[2005,12]]},"abstract":"<jats:p>\n                    The \u03b1\u2010gal epitope (Gal\u03b11\u20103Gal\u03b21\u2010(3)4GlcNAc\u2010R) is abundantly synthesized on glycolipids and glycoproteins of non\u2010primate mammals and New World monkeys by the glycosylation enzyme \u03b11,3galactosyltransferase (\u03b11,3GT). In humans, apes and Old World monkeys, this epitope is absent because the \u03b11,3GT gene was inactivated in ancestral Old World primates. Instead, humans, apes and Old World monkeys produce the anti\u2010Gal antibody, which specifically interacts with \u03b1\u2010gal epitopes and which constitutes \u223c1% of circulating immunoglobulins. Anti\u2010Gal has functioned as an immunological barrier, preventing the transplantation of pig organs into humans, because anti\u2010Gal binds to the \u03b1\u2010gal epitopes expressed on pig cells. The recent generation of \u03b11,3GT knockout pigs that lack \u03b1\u2010gal epitopes has resulted in the elimination of this immunological barrier. Anti\u2010Gal can be exploited for clinical use in cancer immunotherapy by targeting autologous tumour vaccines to APC, thereby increasing their immunogenicity. Autologous intact tumour cells from haematological malignancies, or autologous tumour cell membranes from solid tumours are processed to express \u03b1\u2010gal epitopes by incubation with neuraminidase, recombinant \u03b11,3GT and with uridine diphosphate galactose. Subsequent immunization with such autologous tumour vaccines results in\n                    <jats:italic>in vivo<\/jats:italic>\n                    opsonization by anti\u2010Gal IgG binding to these \u03b1\u2010gal epitopes. The interaction of the Fc portion of the vaccine\u2010bound anti\u2010Gal with Fc\u03b3 receptors of APC induces effective uptake of the vaccinating tumour cell membranes by the APC, followed by effective transport of the vaccinating tumour membranes to the regional lymph nodes, and processing and presentation of the tumour\u2010associated antigen (TAA) peptides. Activation of tumour\u2010specific T cells within the lymph nodes by autologous TAA peptides may elicit an immune response that in some patients will be potent enough to eradicate the residual tumour cells that remain after completion of standard therapy. A similar expression of \u03b1\u2010gal epitopes can be achieved by transduction of tumour cells with an adenovirus vector (or other vectors) containing the \u03b11,3GT gene, thus enabling anti\u2010Gal\u2010mediated targeting of the vaccinating transduced cells to APC. Intratumoral delivery of the \u03b11,3GT gene by various vectors results in the expression of \u03b1\u2010gal epitopes. Such expression of the xenograft carbohydrate phenotype is likely to induce anti\u2010Gal\u2010mediated destruction of the tumour lesion, similar to rejection of xenografts by this antibody. Opsonization of the destroyed tumour cell membranes by anti\u2010Gal IgG further targets them to APC, thus converting the tumour lesion, treated by the \u03b11,3GT gene, into an\n                    <jats:italic>in situ<\/jats:italic>\n                    autologous tumour vaccine.\n                  <\/jats:p>","DOI":"10.1111\/j.1440-1711.2005.01366.x","type":"journal-article","created":{"date-parts":[[2005,9,7]],"date-time":"2005-09-07T04:27:32Z","timestamp":1126067252000},"page":"674-686","source":"Crossref","is-referenced-by-count":311,"title":["The \u03b1\u2010gal epitope and the anti\u2010Gal antibody in xenotransplantation and in cancer immunotherapy"],"prefix":"10.1111","volume":"83","author":[{"given":"Uri","family":"Galili","sequence":"first","affiliation":[{"name":"Division of Hematology\/Oncology, Department of Medicine, University of Massachusetts Medical School  Worcester Massachusetts USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,10,21]]},"reference":[{"key":"e_1_2_6_1_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.160.5.1519"},{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a128881"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.162.2.573"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.165.3.693"},{"key":"e_1_2_6_5_1","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1093\/glycob\/6.6.599","article-title":"Molecular mimicry in the recognition of glycosphingolipids by Gal\u03b13Gal\u03924GlcNAc\u03b2\u2010binding Clostridium difficile toxin A, human natural anti\u2010\u03b1\u2010galactosyl IgG and the monoclonal antibody Gal\u201013: characterization of a binding\u2010active human glycosphingolipid, non\u2010identical with the animal receptor.","volume":"6","author":"Tenebergs S","year":"1996","journal-title":"Glycobiology"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00201098"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00468a024"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.166.2.419"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.56.7.1730-1737.1988"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI106094"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V82.8.2485.2485"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1177\/152216280100400108"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1097\/00007890-199506150-00008"},{"key":"e_1_2_6_14_1","doi-asserted-by":"crossref","first-page":"1276","DOI":"10.4049\/jimmunol.155.3.1276","article-title":"Human anti\u2010Gal heavy chain genes: preferential use of VH3 and the presence of somatic mutations.","volume":"155","author":"Wang L","year":"1995","journal-title":"J. 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