{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T23:32:51Z","timestamp":1771371171017,"version":"3.50.1"},"reference-count":157,"publisher":"MDPI AG","issue":"18","license":[{"start":{"date-parts":[[2020,9,13]],"date-time":"2020-09-13T00:00:00Z","timestamp":1599955200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The glycans on enveloped viruses are synthesized by host-cell machinery. Some of these glycans on zoonotic viruses of mammalian reservoirs are recognized by human natural antibodies that may protect against such viruses. These antibodies are produced mostly against carbohydrate antigens on gastrointestinal bacteria and fortuitously, they bind to carbohydrate antigens synthesized in other mammals, neutralize and destroy viruses presenting these antigens. Two such antibodies are: anti-Gal binding to \u03b1-gal epitopes synthesized in non-primate mammals, lemurs, and New World monkeys, and anti-N-glycolyl neuraminic acid (anti-Neu5Gc) binding to N-glycolyl-neuraminic acid (Neu5Gc) synthesized in apes, Old World monkeys, and many non-primate mammals. Anti-Gal appeared in Old World primates following accidental inactivation of the \u03b11,3galactosyltransferase gene 20\u201330 million years ago. Anti-Neu5Gc appeared in hominins following the inactivation of the cytidine-monophosphate-N-acetyl-neuraminic acid hydroxylase gene, which led to the loss of Neu5Gc &lt;6 million-years-ago. It is suggested that an epidemic of a lethal virus eliminated ancestral Old World-primates synthesizing \u03b1-gal epitopes, whereas few mutated offspring lacking \u03b1-gal epitopes and producing anti-Gal survived because anti-Gal destroyed viruses presenting \u03b1-gal epitopes, following replication in parental populations. Similarly, anti-Neu5Gc protected few mutated hominins lacking Neu5Gc in lethal virus epidemics that eliminated parental hominins synthesizing Neu5Gc. Since \u03b1-gal epitopes are presented on many zoonotic viruses it is suggested that vaccines elevating anti-Gal titers may be of protective significance in areas endemic for such zoonotic viruses. This protection would be during the non-primate mammal to human virus transmission, but not in subsequent human to human transmission where the virus presents human glycans. In addition, production of viral vaccines presenting multiple \u03b1-gal epitopes increases their immunogenicity because of effective anti-Gal-mediated targeting of vaccines to antigen presenting cells for extensive uptake of the vaccine by these cells.<\/jats:p>","DOI":"10.3390\/ijms21186702","type":"journal-article","created":{"date-parts":[[2020,9,13]],"date-time":"2020-09-13T21:11:32Z","timestamp":1600031492000},"page":"6702","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Host Synthesized Carbohydrate Antigens on Viral Glycoproteins as \u201cAchilles\u2019 Heel\u201d of Viruses Contributing to Anti-Viral Immune Protection"],"prefix":"10.3390","volume":"21","author":[{"given":"Uri","family":"Galili","sequence":"first","affiliation":[{"name":"Rush Medical College, Rush University, Chicago, IL 60612, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2020,9,13]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.tim.2007.03.003","article-title":"Virus glycosylation: Role in virulence and immune interactions","volume":"15","author":"Vigerust","year":"2007","journal-title":"Trends Microbiol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1038\/nsmb.3293","article-title":"Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy","volume":"23","author":"Walls","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Xiong, X., Tortorici, M.A., Snijder, J., Yoshioka, C., Walls, A.C., Li, W., McGuire, A.T., Rey, F.A., Bosch, B.J., and Veesler, D. (2018). Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections. J. Virol., 92.","DOI":"10.1128\/JVI.01628-17"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nature01470","article-title":"Antibody neutralization and escape by HIV-1","volume":"422","author":"Wei","year":"2003","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Crooks, E., Tong, T., Chakrabarti, B., Narayan, K., Georgiev, I., and Menis, S. (2015). Vaccine-elicited tier 2 HIV-1 neutralizing antibodies bind to quaternary epitopes involving glycan-deficient patches Proximal to the CD4 Binding Site. PLoS Pathog., 11.","DOI":"10.1371\/journal.ppat.1004932"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"910","DOI":"10.3389\/fimmu.2018.00910","article-title":"Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies","volume":"9","author":"Lavie","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1111\/imr.12507","article-title":"The HIV-1 envelope glycoprotein structure: Nailing down a moving target","volume":"275","author":"Ward","year":"2017","journal-title":"Immunol. Rev."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"BSR20171505","DOI":"10.1042\/BSR20171505","article-title":"Influenza virus N-linked glycosylation and innate immunity","volume":"39","author":"York","year":"2019","journal-title":"Biosci. Rep."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"287","DOI":"10.4049\/jimmunol.66.2.287","article-title":"Origin of naturally occurring hemagglutinins and hemolysins","volume":"66","author":"Wiener","year":"1951","journal-title":"J. Immunol."},{"key":"ref_10","first-page":"9","article-title":"Blood-group and Forssman antigenic determinants shared between microbes and mammalian cells","volume":"15","author":"Springer","year":"1971","journal-title":"Prog. Allergy"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1038\/nchembio.1525","article-title":"Microbial glycan microarrays define key features of host-microbial interactions","volume":"10","author":"Stowell","year":"2014","journal-title":"Nat. Chem. Biol."},{"key":"ref_12","first-page":"786","article-title":"Natural antibodies to glycans","volume":"78","author":"Bovin","year":"2013","journal-title":"Biochemistry"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"17033","DOI":"10.1073\/pnas.0407902101","article-title":"Printed covalent glycan array for ligand profiling of diverse glycan binding proteins","volume":"101","author":"Blixt","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1099\/00222615-13-1-45","article-title":"The microbial contribution to human faecal mass","volume":"13","author":"Stephen","year":"1980","journal-title":"J. Med. Microbiol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/s12263-011-0229-7","article-title":"Intestinal microbiota in human health and disease: The impact of probiotics","volume":"6","author":"Gerritsen","year":"2011","journal-title":"Genes Nutr."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Galili, U. (2020). Human Natural Antibodies to Mammalian Carbohydrate Antigens as Unsung Heroes Protecting Against Past, Present, and Future Viral Infections. Antibodies, 9.","DOI":"10.3390\/antib9020025"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.1073\/pnas.84.5.1369","article-title":"Evolutionary relationship between the anti-Gal antibody and the Gal\u03b11-3Gal epitope in primates","volume":"84","author":"Galili","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"17755","DOI":"10.1016\/S0021-9258(19)77900-9","article-title":"Man, apes, and Old-World monkeys differ from other mammals in the expression of \u03b1-galactosyl epitopes on nucleated cells","volume":"263","author":"Galili","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1034\/j.1399-3089.1999.00008.x","article-title":"Major carbohydrate epitopes in tissues of domestic and African wild animals of potential interest for xenotransplantation research","volume":"6","author":"Oriol","year":"1999","journal-title":"Xenotransplantation"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1016\/S0021-9258(19)44247-6","article-title":"Enzymatic synthesis of blood group related pentaglycosyl ceramide by an \u03b1-galactosyltransferase","volume":"248","author":"Basu","year":"1973","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1519","DOI":"10.1084\/jem.160.5.1519","article-title":"A unique natural human IgG antibody with anti-\u03b1-galactosyl specificity","volume":"160","author":"Galili","year":"1984","journal-title":"J. Exp. Med."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1084\/jem.162.2.573","article-title":"Human natural anti-\u03b1-galactosyl IgG. II. The specific recognition of \u03b1[1,3]-linked galactose residues","volume":"162","author":"Galili","year":"1985","journal-title":"J. Exp. Med."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1084\/jem.166.2.419","article-title":"Circulating antibodies to mouse laminin in Chagas disease, American cutaneous leishmaniasis, and normal individuals recognize terminal galactosyl[\u03b11-3]-galactose epitopes","volume":"166","author":"Towbin","year":"1987","journal-title":"J. Exp. Med."},{"key":"ref_24","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\u00df4GlcNAc\u00df-binding Clostridium difficile toxin A, human natural anti-\u03b1-galactosyl IgG and the monoclonal antibody Gal-13: Characterization of a binding-active human glycosphingolipid, non-identical with the animal receptor","volume":"6","author":"Teneberg","year":"1996","journal-title":"Glycobiology"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1093\/glycob\/9.9.865","article-title":"Naturally occurring anti-\u03b1-galactosyl antibodies: Relationship to xenoreactive anti-\u03b1-galactosyl antibodies","volume":"9","author":"Parker","year":"1999","journal-title":"Glycobiology"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1023\/A:1020506617105","article-title":"Immunochemical properties of anti-Gal\u03b11-3Gal antibodies after sensitization with xenogeneic tissues","volume":"19","author":"Yu","year":"1999","journal-title":"J. Clin. Immunol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1097\/00007890-199708150-00021","article-title":"Heterogeneity of human anti-pig natural antibodies cross-reactive with the Gal[\u03b11,3]Galactose epitope","volume":"64","author":"McMorrow","year":"1997","journal-title":"Transplantation"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1128\/cdli.2.2.125-131.1995","article-title":"Human secretions contain IgA, IgG and IgM anti-Gal [anti-\u03b1-galactosyl] antibodies","volume":"2","author":"Hamadeh","year":"1995","journal-title":"Clin. Diagn. Lab. Immunol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1056\/NEJMoa074943","article-title":"Cetuximab-induced anaphylaxis and IgE specific for galactose-\u03b1-1,3-galactose","volume":"358","author":"Chung","year":"2008","journal-title":"N. Engl. J. Med."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1016\/j.jaci.2020.01.047","article-title":"On the cause and consequences of IgE to galactose-\u03b1-1,3-galactose: A report from the National Institute of Allergy and Infectious Diseases Workshop on Understanding IgE-Mediated Mammalian Meat Allergy","volume":"145","author":"Commins","year":"2020","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1662","DOI":"10.1016\/j.jaci.2016.04.010","article-title":"IgE in the diagnosis and treatment of allergic disease","volume":"137","author":"Schuyler","year":"2016","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.3389\/fimmu.2019.01210","article-title":"Environmental and Molecular Drivers of the \u03b1-gal Syndrome","volume":"10","author":"Duscher","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1730","DOI":"10.1128\/iai.56.7.1730-1737.1988","article-title":"Interaction between human natural anti-\u03b1-galactosyl immunoglobulin G and bacteria of the human flora","volume":"56","author":"Galili","year":"1988","journal-title":"Infect. Immun."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"4611","DOI":"10.1038\/s41598-020-61632-9","article-title":"Abundant human anti-Gal\u03b13Gal antibodies display broad pathogen reactivity","volume":"10","author":"Petersen","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"6215","DOI":"10.1128\/IAI.70.11.6215-6222.2002","article-title":"Induction of cytolytic anti-Gal antibodies in \u03b1-1,3-galactosyltransferase gene knockout mice by oral inoculation with Escherichia coli O86:B7 bacteria","volume":"70","author":"Posekany","year":"2002","journal-title":"Infect. Immun."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1034\/j.1399-3089.2001.00082.x","article-title":"Removal of bowel aerobic gram-negative bacteria is more effective than immunosuppression with cyclophosphamide and steroids to decrease natural \u03b1-galactosyl IgG antibodies","volume":"8","author":"Blanco","year":"2001","journal-title":"Xenotransplantation"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"5804","DOI":"10.1021\/bi300640b","article-title":"The wciN gene encodes an \u03b1-1,3-galactosyltransferase involved in the biosynthesis of the capsule repeating unit of Streptococcus pneumoniae serotype 6B","volume":"51","author":"Han","year":"2012","journal-title":"Biochemistry"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.carres.2019.02.003","article-title":"Impact of branching on the conformational heterogeneity of the lipopolysaccharide from Klebsiella pneumoniae: Implications for vaccine design","volume":"475","author":"Aytenfisu","year":"2019","journal-title":"Carbohydr. Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1146\/annurev.iy.13.040195.003255","article-title":"T cell independent antigens type 2","volume":"13","author":"Mond","year":"1995","journal-title":"Annu. Rev. Immunol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1172\/JCI91192","article-title":"T cells control the generation of nanomolar-affinity anti-glycan antibodies","volume":"127","author":"Polonskaya","year":"2017","journal-title":"J. Clin. Investig."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1172\/JCI7358","article-title":"Differential immune responses to \u03b1-gal epitopes on xenografts and allografts: Implications for accommodation in xenotransplantation","volume":"105","author":"Tanemura","year":"2000","journal-title":"J. Clin. Investig."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1097\/01.TP.0000142673.32394.95","article-title":"Immune response, accommodation and tolerance to transplantation carbohydrate antigens","volume":"78","author":"Galili","year":"2004","journal-title":"Transplantation"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"2485","DOI":"10.1182\/blood.V82.8.2485.2485","article-title":"One percent of circulating B lymphocytes are capable of producing the natural anti-Gal antibody","volume":"82","author":"Galili","year":"1993","journal-title":"Blood"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1097\/00007890-199506150-00008","article-title":"Increased anti-Gal activity in diabetic patients transplanted with fetal porcine islet cell clusters","volume":"59","author":"Galili","year":"1995","journal-title":"Transplantation"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.arthro.2006.12.024","article-title":"Anterior cruciate ligament reconstruction with a porcine xenograft: A serologic, histologic, and biomechanical study in primates","volume":"23","author":"Stone","year":"2007","journal-title":"Arthroscopy"},{"key":"ref_46","unstructured":"Galili, U. (2018). The Natural Anti-Gal Antibody As Foe Turned Friend in Medicine, Elsevier\/Academic Press."},{"key":"ref_47","first-page":"559","article-title":"Identification of carbohydrate structures which bind human anti-porcine antibodies: Implication for discordant xenografting in man","volume":"24","author":"Good","year":"1992","journal-title":"Transplant. Proc."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1016\/0167-5699(93)90261-I","article-title":"Interaction of the natural anti-Gal antibody with \u03b1-galactosyl epitopes: A major obstacle for xenotransplantation in humans","volume":"14","author":"Galili","year":"1993","journal-title":"Immunol. Today"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"11391","DOI":"10.1073\/pnas.90.23.11391","article-title":"Anti-pig IgM antibodies in human serum react predominantly with Gal (\u03b1l-3)Gal epitopes","volume":"90","author":"Sandrin","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/0966-3274(93)90047-C","article-title":"Identification of \u03b1-galactosyl and other carbohydrate epitopes that are bound by human anti-pig antibodies: Relevance to discordant xenografting in man","volume":"1","author":"Cooper","year":"1993","journal-title":"Transpl. Immunol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"5500","DOI":"10.4049\/jimmunol.154.10.5500","article-title":"Cardiac xenografts between primate species provide evidence for the importance of the \u03b1-galactosyl determinant in hyperacute rejection","volume":"154","author":"Collins","year":"1995","journal-title":"J. Immunol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1097\/00007890-199802150-00009","article-title":"Intravenous infusion of Gal\u03b11-3Gal oligosaccharides in baboon delays hyperacute rejection of porcine heart xenografts","volume":"56","author":"Simon","year":"1998","journal-title":"Transplantation"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1097\/00007890-199801270-00005","article-title":"Removal of anti-porcine natural antibodies from human and nonhuman primate plasma in vitro and in vivo by a Gal\u03b11-3Gal\u03b21-4Glc\u03b2-X immunoaffinity column","volume":"65","author":"Xu","year":"1998","journal-title":"Transplantation"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1480","DOI":"10.1016\/j.bbagen.2019.05.012","article-title":"Exploitation of glycosylation in enveloped virus pathobiology","volume":"1863","author":"Watanabe","year":"2019","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1099\/0022-1317-75-5-1177","article-title":"Differential host dependent expression of \u03b1-galactosyl epitopes on viral glycoproteins: A study of Eastern equine encephalitis virus as a model","volume":"75","author":"Repik","year":"1994","journal-title":"J. Gen. Virol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/0264-410X(95)00189-8","article-title":"Enhancement of antigen presentation of influenza virus hemagglutinin by the natural anti-Gal antibody","volume":"14","author":"Galili","year":"1996","journal-title":"Vaccine"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"5628","DOI":"10.1021\/bi00318a038","article-title":"Major oligosaccharides in the glycoprotein of Friend murine leukemia virus: Structure elucidation by one- and two-dimensional proton nuclear magnetic resonance and methylation analysis","volume":"23","author":"Geyer","year":"1984","journal-title":"Biochemistry"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1084\/jem.182.5.1345","article-title":"A novel mechanism of retrovirus inactivation in human serum mediated by anti-\u03b1-galactosyl natural antibody","volume":"182","author":"Rother","year":"1995","journal-title":"J. Exp. Med."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1038\/379085a0","article-title":"Sensitization of cells and retroviruses to human serum by (\u03b11-3) galactosyltransferase","volume":"379","author":"Takeuchi","year":"1996","journal-title":"Nature"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virusres.2003.09.008","article-title":"The neutralization of pseudorabies virus by anti-\u03b1-galactosyl natural antibody in normal serum","volume":"99","author":"Hayashi","year":"2004","journal-title":"Virus Res."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"6174","DOI":"10.1128\/jvi.71.8.6174-6178.1997","article-title":"Sensitization of rhabdo-, lenti-, and spumaviruses to human serum by galactosyl(\u03b11-3)galactosylation","volume":"71","author":"Takeuchi","year":"1997","journal-title":"J. Virol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"4650","DOI":"10.1128\/JVI.72.6.4650-4656.1998","article-title":"Evaluation of the Gal\u03b11-3Gal epitope as a host modification factor eliciting natural humoral immunity to enveloped viruses","volume":"72","author":"Welsh","year":"1998","journal-title":"J. Virol."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Pipperger, L., Koske, I., Wild, N., M\u00fcllauer, B., Krenn, D., Stoiber, H., Wollmann, G., Kimpel, J., von Laer, D., and B\u00e1nki, Z. (2019). Xenoantigen-dependent complement-mediated neutralization of LCMV glycoprotein pseudotyped VSV in human serum. J. Virol., 93.","DOI":"10.1128\/JVI.00567-19"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2477","DOI":"10.1182\/blood.V99.7.2477","article-title":"Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement","volume":"99","author":"Preece","year":"2002","journal-title":"Blood"},{"key":"ref_65","first-page":"1254","article-title":"Virus recognition by specific natural antibodies and complement results in MHC I cross-presentation","volume":"37","author":"Baple","year":"2007","journal-title":"J. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1111\/j.1399-3089.2007.00377.x","article-title":"Natural protection from zoonosis by \u03b1-gal epitopes on virus particles in xenotransmission","volume":"14","author":"Kim","year":"2007","journal-title":"Xenotransplantation"},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Yan, L.M., Lau, S.P.N., Poh, C.M., Chan, V.S.F., Chan, M.C.W., Peiris, M., and Poon, L.L.M. (2020). Heterosubtypic Protection Induced by a Live Attenuated Influenza Virus Vaccine Expressing Galactose-\u03b1-1,3-Galactose Epitopes in Infected Cells. mBio, 11.","DOI":"10.1128\/mBio.00027-20"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1126\/science.285.5431.1236","article-title":"Search for cross-species transmission of porcine endogenous retrovirus in patients treated with living pig tissue","volume":"285","author":"Paradis","year":"1999","journal-title":"Science"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1038\/nm0397-282","article-title":"Infection of human cells by an endogenous retrovirus of pigs","volume":"3","author":"Patience","year":"1997","journal-title":"Nat. Med."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"21437","DOI":"10.1074\/jbc.270.37.21437","article-title":"Oocyte Gal\u03b11,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse","volume":"270","author":"Thall","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"9131","DOI":"10.1128\/JVI.00647-07","article-title":"Increased immunogenicity of influenza virus vaccine by anti-Gal mediated targeting to antigen presenting cells","volume":"81","author":"Guay","year":"2007","journal-title":"J. Virol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1016\/S0264-410X(96)00300-3","article-title":"Synthesis of \u03b1-gal epitopes on influenza virus vaccines, by recombinant \u03b11,3galactosyltransferase, enables the formation of immune complexes with the natural anti-Gal antibody","volume":"15","author":"Henion","year":"1997","journal-title":"Vaccine"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"6943","DOI":"10.1128\/JVI.00310-06","article-title":"Increased immunogenicity of human immunodeficiency virus gp120 engineered to express Gal\u03b11-3Gal\u03b21-4GlcNAc-R epitopes","volume":"80","author":"Wang","year":"2006","journal-title":"J. Virol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2638","DOI":"10.1002\/eji.200526146","article-title":"The influence of natural antibody specificity on antigen immunogenicity","volume":"35","author":"Benatuil","year":"2005","journal-title":"Eur. J. Immunol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"3072","DOI":"10.1016\/j.vaccine.2009.03.019","article-title":"Mechanism for increased immunogenicity of vaccines that form in-vivo immune complexes with the natural anti-Gal antibody","volume":"27","author":"Wigglesworth","year":"2009","journal-title":"Vaccine"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1034\/j.1399-3089.1999.00023.x","article-title":"Quantitation and characterization of anti-Gal\u03b11-3Gal antibodies in sera of 200 healthy persons","volume":"6","author":"Buonomano","year":"1999","journal-title":"Xenotransplantation"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1084\/jem.165.3.693","article-title":"The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by crossreactivity between natural anti-Gal and anti-B antibodies","volume":"165","author":"Galili","year":"1987","journal-title":"J. Exp. Med."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Breiman, A., Ruv\u00ebn-Clouet, N., and Le Pendu, J. (2020). Harnessing the natural anti-glycan immune response to limit the transmission of enveloped viruses such as SARS-CoV-2. PLoS Pathog., 16.","DOI":"10.1371\/journal.ppat.1008556"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1021\/acscentsci.7b00517","article-title":"Immunity to \u03b1-gal: Toward a single-antigen pan-vaccine to control major infectious diseases","volume":"3","year":"2017","journal-title":"ACS Cent. Sci."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1038\/s41541-019-0107-7","article-title":"A prophylactic \u03b1-gal-based glycovaccine effectively protects against murine acute Chagas disease","volume":"4","author":"Portillo","year":"2019","journal-title":"NPJ Vaccines"},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Iniguez, E., Schocker, N.S., Subramaniam, K., Portillo, S., Montoya, A.L., Al-Salem, W.S., Torres, C.L., Rodriguez, F., Moreira, O.C., and Acosta-Serranoet, A. (2017). An \u03b1-gal-containing neoglycoprotein-based vaccine partially protects against murine cutaneous leishmaniasis caused by Leishmania major. PLoS Negl. Trop. Dis., 11.","DOI":"10.1371\/journal.pntd.0006039"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1016\/j.cell.2014.10.053","article-title":"Gut microbiota elicits a protective immune response against malaria transmission","volume":"159","author":"Yilmaz","year":"2014","journal-title":"Cell"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"7055","DOI":"10.1016\/S0021-9258(19)39258-0","article-title":"Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal:\u03b2-D-Gal[1,4]-D-GlcNAc \u03b1[1,3]-galactosyltransferase cDNA","volume":"265","author":"Larsen","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"7401","DOI":"10.1073\/pnas.88.16.7401","article-title":"Gene sequences suggest inactivation of \u03b11-3 galactosyltransferase in catarrhines after the divergence of apes from monkeys","volume":"88","author":"Galili","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1093\/glycob\/4.2.193","article-title":"Defining the minimal size of catalytically active primate \u03b11,3galactosyltransferase: Structure function studies on the recombinant truncated enzyme","volume":"4","author":"Henion","year":"1994","journal-title":"Glycobiology"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"10114","DOI":"10.1074\/jbc.M110527200","article-title":"Molecular basis of evolutionary loss of the \u03b11,3-galactosyltransferase gene in higher primates","volume":"277","author":"Koike","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1093\/glycob\/cwf087","article-title":"A complete \u03b11,3-galactosyltransferase gene is present in the human genome and partially transcribed","volume":"12","author":"Lanteri","year":"2002","journal-title":"Glycobiology"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1034\/j.1399-3089.2002.1o058.x","article-title":"Anti-Gal\u03b11-3Gal IgM and IgG antibody levels in sera of humans and old world non-human primates","volume":"9","author":"Teranishi","year":"2002","journal-title":"Xenotransplantation"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1002\/ajpa.23745","article-title":"Evolution in primates by \u201cCatastrophic-selection\u201d interplay between enveloped virus epidemics, mutated genes of enzymes synthesizing carbohydrate antigens, and natural anti-carbohydrate antibodies","volume":"168","author":"Galili","year":"2019","journal-title":"Am. J. Phys. Anthropol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"257","DOI":"10.2307\/2406275","article-title":"Catastrophic selection as a factor in speciation","volume":"16","author":"Lewis","year":"1962","journal-title":"Evolution"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1126\/science.1068228","article-title":"Production of \u03b1-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning","volume":"295","author":"Lai","year":"2002","journal-title":"Science"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1126\/science.1078942","article-title":"Production of \u03b11,3-galactosyltransferase-deficient pigs","volume":"299","author":"Phelps","year":"2003","journal-title":"Science"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1097\/01.TP.0000130487.68051.EB","article-title":"\u03b11,3-Galactosyltransferase gene-knockout miniature swine produce natural cytotoxic anti-Gal antibodies","volume":"78","author":"Dor","year":"2004","journal-title":"Transplantation"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1111\/j.1399-3089.2012.00710.x","article-title":"Anti-gal antibodies in \u03b11,3-galactosyltransferase gene knockout pigs","volume":"19","author":"Fang","year":"2012","journal-title":"Xenotransplantation"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1111\/xen.12051","article-title":"\u03b11,3Galactosyltransferase knockout pigs produce the natural anti-Gal antibody and simulate the evolutionary appearance of this antibody in primates","volume":"20","author":"Galili","year":"2013","journal-title":"Xenotransplantation"},{"key":"ref_96","first-page":"903","article-title":"A new blood group character related to the ABO system","volume":"1","author":"Bhende","year":"1952","journal-title":"Lancet"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1111\/j.1423-0410.1974.tb02450.x","article-title":"Incidence of Bombay Oh phenotype and weaker variants of A and B antigens in Bombay (India)","volume":"27","author":"Bhatia","year":"1974","journal-title":"Vox Sang."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/0014-5793(77)81060-0","article-title":"Activity of 2-\u03b1-L-fucosyltransferase in human sera and red cell membranes. Study of common ABH blood donors, rare \u2018Bombay\u2019 and \u2018Parabombay\u2019 individuals","volume":"84","author":"Mulet","year":"1977","journal-title":"FEBS Lett."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1080\/09723757.2005.11885925","article-title":"Detection of a rare blood group \u201cBombay (Oh) Phenotype\u201d among the Kutia Kondh primitive tribe of Orissa, India","volume":"5","author":"Balgir","year":"2005","journal-title":"Int. J. Hum. Genet."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1515\/bchm3.1988.369.1.477","article-title":"The biosynthesis of N-glycoloylneuraminic acid occurs by hydroxylation of the CMP-glycoside of N-acetylneuraminic acid","volume":"369","author":"Shaw","year":"1988","journal-title":"Biol. Chem. Hoppe-Seyler"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1002\/(SICI)1096-8644(199810)107:2<187::AID-AJPA5>3.0.CO;2-S","article-title":"A structural difference between the cell surfaces of humans and the great apes","volume":"107","author":"Muchmore","year":"1998","journal-title":"Am. J. Phys. Anthropol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"8939","DOI":"10.1073\/pnas.0914634107","article-title":"Colloquium paper: Uniquely human evolution of sialic acid genetics and biology","volume":"107","author":"Varki","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"11751","DOI":"10.1073\/pnas.95.20.11751","article-title":"A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence","volume":"95","author":"Chou","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"15866","DOI":"10.1074\/jbc.273.25.15866","article-title":"The molecular basis for the absence of N-glycolylneuraminic acid in humans","volume":"273","author":"Irie","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1159\/000232140","article-title":"Characterization of the Hanganutziu-Deicher (serum-sickness) antigen as gangliosides containing N-glycolylneuraminic acid","volume":"57","author":"Merrick","year":"1978","journal-title":"Int. Arch. Allergy Appl. Immunol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1034\/j.1399-3089.2002.02138.x","article-title":"Anti-N-glycolylneuraminic acid antibodies identified in healthy human serum","volume":"9","author":"Zhu","year":"2002","journal-title":"Xenotransplantation"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1093\/glycob\/cwn072","article-title":"Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: Potential implications for disease","volume":"18","author":"Yu","year":"2008","journal-title":"Glycobiology"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"807","DOI":"10.3389\/fimmu.2019.00807","article-title":"From \u201cSerum Sickness\u201d to \u201cXenosialitis\u201d: Past, Present, and Future Significance of the Non-human Sialic Acid Neu5Gc","volume":"10","author":"Dhar","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"789","DOI":"10.3389\/fimmu.2019.00789","article-title":"Absence of Neu5Gc and Presence of Anti-Neu5Gc Antibodies in Humans-An Evolutionary Perspective","volume":"10","author":"Altman","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"2907","DOI":"10.4049\/jimmunol.1301195","article-title":"Long-term IgG response to porcine Neu5Gc antigens without transmission of PERV in burn patients treated with porcine skin xenografts","volume":"191","author":"Scobie","year":"2013","journal-title":"J. Immunol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1093\/glycob\/9.8.747","article-title":"Evolutionary considerations in relating oligosaccharide diversity to biological function","volume":"9","author":"Gagneux","year":"1999","journal-title":"Glycobiology"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1128\/CMR.00109-14","article-title":"Blood Groups in Infection and Host Susceptibility","volume":"28","author":"Cooling","year":"2015","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1098\/rspb.2004.2674","article-title":"Evolution of the human ABO polymorphism by two complementary selective pressures","volume":"271","author":"Seymour","year":"2004","journal-title":"Proc. Biol. Sci."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"4693","DOI":"10.1182\/blood-2004-11-4267","article-title":"HIV-1 incorporates ABO histo-blood group antigens that sensitize virions to complement-mediated inactivation","volume":"105","author":"Neil","year":"2005","journal-title":"Blood"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1093\/glycob\/cwn093","article-title":"Inhibition of the interaction between the SARS-CoV spike protein and its cellular receptor by anti-histo-blood group antibodies","volume":"18","author":"Guillon","year":"2008","journal-title":"Glycobiology"},{"key":"ref_116","first-page":"1450","article-title":"ABO blood group and susceptibility to severe acute respiratory syndrome","volume":"293","author":"Cheng","year":"2005","journal-title":"JAMA"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.cca.2020.06.026","article-title":"Relationship between ABO blood group distribution and clinical characteristics in patients with COVID-19","volume":"509","author":"Wu","year":"2020","journal-title":"Clin. Chim. Acta"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1111\/bjh.16797","article-title":"Association between ABO blood groups and risk of SARS-CoV-2 pneumonia","volume":"190","author":"Li","year":"2020","journal-title":"Br. J. Haematol."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Zhao, J., Yang, Y., Huang, H., Li, D., Gu, D., Lu, X., Zhang, Z., Liu, L., Liu, T., and Liu, Y. (2020). Relationship between the ABO Blood Group and the COVID-19 Susceptibility. [published online ahead of print, 2020 Aug 4]. Clin. Infect. Dis., ciaa1150.","DOI":"10.1093\/cid\/ciaa1150"},{"key":"ref_120","unstructured":"Mourant, A.E., Kopec, A.C., and Domaniewska-Sobczak, O. (1976). The Distribution of Blood Groups and Other Polymorphisms, Oxford Press. [2nd ed.]."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1002\/ajpa.1330150407","article-title":"The blood groups of South American Indians","volume":"15","author":"Salzano","year":"1957","journal-title":"Am. J. Phys. Anthropol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1111\/j.1423-0410.1994.tb01255.x","article-title":"Molecular bases of the ABO blood groups of Indians from the Brazilian Amazon region","volume":"67","author":"Franco","year":"1994","journal-title":"Vox Sang."},{"key":"ref_123","first-page":"700","article-title":"The blood groups of the Seneca Indians","volume":"19","author":"Doeblin","year":"1967","journal-title":"Am. J. Hum. Genet."},{"key":"ref_124","first-page":"86","article-title":"Blood groups of Caddoan Indians of Oklahoma","volume":"12","author":"Gray","year":"1960","journal-title":"Am. J. Hum. Genet."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1002\/ajpa.1330490121","article-title":"ABO blood groups in Chilean and Peruvian mummies. II. Results of agglutination-inhibition technique","volume":"49","author":"Allison","year":"1978","journal-title":"Am. J. Phys. Anthropol."},{"key":"ref_126","first-page":"937","article-title":"H-deficient blood groups (Bombay) of R\u00e9union Island","volume":"34","author":"Gerard","year":"1982","journal-title":"Am. J. Hum. Genet."},{"key":"ref_127","first-page":"497","article-title":"H-deficient blood groups of Reunion Island. III. \u03b1-2-L-fucosyltransferase activity in sera of homozygous and heterozygous individuals","volume":"35","author":"Cartron","year":"1983","journal-title":"Am. J. Hum. Genet."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1159\/000491880","article-title":"The First Comprehensive Study of H-Deficient Phenotypes in Iran","volume":"46","author":"Shahverdi","year":"2019","journal-title":"Transfus. Med. Hemother."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"6674","DOI":"10.1073\/pnas.87.17.6674","article-title":"Molecular cloning, sequence, and expression of a human GDP-l-fucose:\u03b2-d-galactoside 2-\u03b1-l-fucosyltransferase cDNA that can form the H blood group antigen","volume":"87","author":"Larsen","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"4632","DOI":"10.1074\/jbc.270.9.4632","article-title":"Molecular cloning of a human genomic region containing the H blood group \u03b1(1,2)fucosyltransferase gene and two H locus-related DNA restriction fragments. Isolation of a candidate for the human Secretor blood group locus","volume":"270","author":"Rouquier","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"4640","DOI":"10.1074\/jbc.270.9.4640","article-title":"Sequence and expression of a candidate for the human Secretor blood group \u03b1(1,2)fucosyltransferase gene (FUT2). Homozygosity for an enzyme-inactivating nonsense mutation commonly correlates with the non-secretor phenotype","volume":"270","author":"Kelly","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"5843","DOI":"10.1073\/pnas.91.13.5843","article-title":"Molecular basis for H blood group deficiency in Bombay (Oh) and para-Bombay individuals","volume":"91","author":"Kelly","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1182\/blood.V90.2.839","article-title":"Wide variety of point mutations in the H gene of Bombay and para-Bombay individuals that inactivate H enzyme","volume":"90","author":"Kaneko","year":"1997","journal-title":"Blood"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1006\/bbrc.1997.7232","article-title":"Missense mutation of FUT1 and deletion of FUT2 are responsible for Indian Bombay phenotype of ABO blood group system","volume":"238","author":"Koda","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1046\/j.1537-2995.1997.37397240210.x","article-title":"Polymorphism of the h allele and the population frequency of sporadic nonfunctional alleles","volume":"37","author":"Wagner","year":"1997","journal-title":"Transfusion"},{"key":"ref_136","first-page":"105","article-title":"Molecular genetics of H","volume":"78","author":"Oriol","year":"2000","journal-title":"Vox Sang."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"2149","DOI":"10.1111\/j.1537-2995.2006.01045.x","article-title":"Identification of six new alleles at the FUT1 and FUT2 loci in ethnically diverse individuals with Bombay and ParaBombay phenotypes","volume":"46","author":"Storry","year":"2006","journal-title":"Transfusion"},{"key":"ref_138","first-page":"536","article-title":"The Bombay blood group: Are we out of risk?","volume":"20","author":"Dipta","year":"2011","journal-title":"Mymensingh Med. J."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1007\/s12288-013-0277-9","article-title":"Acute Hemolytic Transfusion Reaction in a Patient with Bombay Phenotype: Implications for ABO Grouping","volume":"30","author":"Malhotra","year":"2014","journal-title":"Indian J. Hematol. Blood Transfus."},{"key":"ref_140","first-page":"89","article-title":"Managing rare blood group requests-Bombay Oh phenotype: Our experience with www.bombaybloodgroup.org","volume":"14","author":"Agarwal","year":"2016","journal-title":"Blood Transfus."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1084\/jem.189.2.371","article-title":"Fc\u03b3 receptor-mediated induction of dendritic cell maturation and major histocompatibility complex class I-restricted antigen presentation after immune complex internalization","volume":"189","author":"Regnault","year":"1999","journal-title":"J. Exp. Med."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"2240","DOI":"10.4049\/jimmunol.168.5.2240","article-title":"Antigen-antibody immune complexes empower dendritic cells to efficiently prime specific CD8+ CTL responses in vivo","volume":"168","author":"Schuurhuis","year":"2002","journal-title":"J. Immunol."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Galili, U. (2020). Amplifying immunogenicity of prospective Covid-19 vaccines by glycoengineering the coronavirus glycan-shield to present \u03b1-gal epitopes. Vaccine, in press.","DOI":"10.1016\/j.vaccine.2020.08.032"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/S0167-5699(97)80024-2","article-title":"Natural anti-Gal antibody as a universal augmenter of autologous tumor vaccine immunogenicity","volume":"18","author":"Galili","year":"1997","journal-title":"Immunol. Today"},{"key":"ref_145","first-page":"3417","article-title":"Increased immunogenicity of tumor vaccines complexed with anti-Gal: Studies in knockout mice for \u03b11,3galactosyltransferase","volume":"59","author":"LaTemple","year":"1999","journal-title":"Cancer Res."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"4676","DOI":"10.4049\/jimmunol.178.7.4676","article-title":"Intratumoral injection of \u03b1-gal glycolipids induces xenograft-like destruction and conversion of lesions into endogenous vaccines","volume":"178","author":"Galili","year":"2007","journal-title":"J. Immunol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1093\/glycob\/11.7.577","article-title":"Synthesis of \u03b1-gal epitopes (Gal\u03b11-3Gal\u03b21-4GlcNAc-R) on human tumor cells by recombinant \u03b11,3galactosyltransferase produced in Pichia pastoris","volume":"11","author":"Chen","year":"2001","journal-title":"Glycobiology"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.1016\/j.vaccine.2009.12.015","article-title":"Increased immunogenicity of HIV-1 p24 and gp120 following immunization with gp120\/p24 fusion protein vaccine expressing \u03b1-gal epitopes","volume":"28","author":"Wang","year":"2010","journal-title":"Vaccine"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"6225","DOI":"10.1016\/S0021-9258(19)39314-7","article-title":"Transfer and expression of a murine UDP-Gal:\u03b2-d-Gal-\u03b11,3-galactosyltransferase gene in transfected Chinese hamster ovary cells. Competition reactions between the \u03b11,3-galactosyltransferase and the endogenous \u03b12,3-sialyltransferase","volume":"265","author":"Smith","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1093\/glycob\/12.2.135","article-title":"Expression of \u03b1-gal epitopes on HeLa cells transduced with adenovirus containing \u03b11,3galactosyltransferase cDNA","volume":"12","author":"Deriy","year":"2002","journal-title":"Glycobiology"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"5022","DOI":"10.1073\/pnas.0931263100","article-title":"Use of combinatorial genetic libraries to humanize N-linked glycosylation in the yeast Pichia pastoris","volume":"100","author":"Choi","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/nrmicro1087","article-title":"The humanization of N-glycosylation pathways in yeast","volume":"3","author":"Wildt","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/s00253-010-2718-9","article-title":"Extracellular accumulation of recombinant protein by Escherichia coli in a defined medium","volume":"88","author":"Fu","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1128\/AEM.01901-10","article-title":"Production of secretory and extracellular N-linked glycoproteins in Escherichia coli","volume":"77","author":"Fisher","year":"2011","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"31594","DOI":"10.1074\/jbc.M004005200","article-title":"Changing the donor cofactor of bovine \u03b11,3-galactosyltransferase by fusion with UDP-galactose 4-epimerase","volume":"275","author":"Chen","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.carres.2012.05.015","article-title":"Synthesis of \u03b1-galactosyl epitopes by metabolically engineered Escherichia coli","volume":"361","author":"Gebus","year":"2012","journal-title":"Carbohydr. Res."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"1790","DOI":"10.1126\/science.298.5599.1790","article-title":"N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli","volume":"298","author":"Wacker","year":"2002","journal-title":"Science"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/18\/6702\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T10:09:35Z","timestamp":1760177375000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/18\/6702"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,9,13]]},"references-count":157,"journal-issue":{"issue":"18","published-online":{"date-parts":[[2020,9]]}},"alternative-id":["ijms21186702"],"URL":"https:\/\/doi.org\/10.3390\/ijms21186702","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,9,13]]}}}