Abstract
The α-gal epitope (Galα1,3Galβl,4GlcNAc-R) is a terminal glycosidic structure that is expressed on the surface of cells from most mammalian species other than humans, apes and Old World monkeys (Galili et al., 1988a; Galili et al., 1987). The terminal α-galactosyl unit of this epitope is added to nascent glycolipids and glycoproteins in the Golgi apparatus by α1,3galactosyltransferase (α1,3GT). In primates lacking the α-gal epitope, the α1,3GT gene is not transcribed, and nonsense mutations are present within the coding region of some species (Galili and Swanson, 1991; Larsen et al., 1990a; Joziasse et al., 1989). The presence of a functional α1,3GT in New World monkeys suggests that this gene was inactivated in ancestral Old World monkeys and apes after their divergence from New World monkeys (Galili et al., 1988a). A detailed comparison of the α1,3GT pseudogene sequences in Old World monkeys and apes further suggests that this gene was inactivated after these two groups diverged from each other (Galili and Andrews, 1995; Galili and Swanson, 1991).
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References
Aaronson, S.A. and Todaro, G.J., 1970. Transformation and virus growth by murine sarcoma viruses in human cells, Nature 225:458–459.
Air, G.M. and Laver, W.G., 1990, Influenza Viruses, in: lmmunochemistry of Viruses. II. The Basis for Serodiagnosis, and Vaccines (M.H. V. van Regemorted. and A.R. Neurath, eds.), Elsevier Science Publications, Amsterdam, pp. 171–216.
Almeida, I.C., Milani, S.R., Gorin, A.J., and Travoassos, L.R., 1991, Complement-mediated lysis of Trypanosoma cruzi tryptomastigotes by human anti α-galactosyl antibodies, J. Immunol. 146:2394–2400.
Anderson, W.A., 1992, Human gene therapy, Science 256:808–813.
Avila, J.L., Rojas, M., and Galili, U., 1989, Immunogenic Galα 1–3Gal carbohydrate epitopes are present on pathogenic American Trypanosoma and Leishmania, J. Immunol. 142:2828–2834.
Banapour, B., Sernatinger, J., and Levy, J.A., 1986, The AIDS-associated retrovirus is not sensitive to lysis or inactivation by human serum, Virol. 152:268–271.
Barbacid, M., Bolognesi, D., and Aaronson, S.A., 1980, Humans have antibodies capable of recognizing oncoviral glycoproteins: demonstration that these antibodies are formed in response to cellular modification of glycoproteins rather than as consequence of exposure to virus, Proc. Natl. Acad. Sci. USA 77:1617–1621.
Bartholomew, R.M., Esser, A.F.,and Muller-Eberhard, H.J., 1978, Lysis of oncornaviruses by human serum: isolation ofthe viral complement (Cl) receptor and identification aspl5E,J. Exp. Med. 147:844–53.
Basu, M. and Basu, S., 1973, Enzymatic synthesis of a blood group-related pentaglycosyl ceramide by an α-galactosyltransferase from rabbit bone marrow, J. Biol. Chem. 248:1700–1706.
Betteridge, A. and Watkins, W.M., 1983, Two α-2-D-galactosyltransferases in rabbit stomach mucosa with different acceptor substrate specificities, Eur. J. Biochem. 132:29–35.
Blake, D.D. and Goldstein, I.J., 1981, An α-D-galactosyltransferase in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide [α-D-galactose (1–3)-N-acetyllactosamine], J. Biol. Chem. 256:5387–5393.
Blanken, W.M. and Ban den Eijnden, D.H., 1985, Biosynthesis of terminal Galα 1–3Galβ 1–4GIcNAc-R oligosaccharide sequence on glycoconjugates: purification and acceptor specificity of a UDP-Gal: N-acetyllactosaminide α 1-3 galactosyltransferase, J. Biol. Chem. 260:12927–12934.
Boiron, R.R., Bernard, C., and Chuat, J.C., 1969, Replication of mouse sarcoma virus Moloney strain (MSV-N) in human cells, Proc. Amer. Assoc. Cancer Res. 10:8.
Burke, D.J. and Keegstra, K., 1976, Purification and composition ofthe proteins from Sindbis virus grown in chick and BHK cells, J. Virol. 20:676–686.
Cardoso, J.E., Branchereau, S., Jeyaraj, P.R., Houssin, D., Danos, O., and Heard, J.-M., 1993, In situ retrovirus-mediated gene transfer into dog liver, Hum. Gene Ther. 4:411–418.
Chang, G.-J.J. and Trent, D.W., 1987, Nucleotide sequence of the genome region encoding the 26S mRNA of eastern equine encephalomyelitis virus and the deduced amino acid sequence of the viral structural proteins, J. Gen. Virol. 68:2129–2142.
Cooper, N.R., Jensen, F.C., Welsh, R.M., Jr., and Oldstone, M.B. A., 1976, Lysis of RN A tumor viruses by human serum: direct antibody-independent triggering ofthe classical complement pathway, J. Exp. Med. 144:970–984.
Cornetta, K., Moen, R.C., Culver, K., Morgan, R.A., McLachlin, J.R., Stu S., Selegue, J., London, W., Blaese, R.M., and Anderson, W.F., 1990, Amphotropic murine leukemia retrovirus is not an acute pathogen for primates, Hum. Gene Ther. 1:15–30.
Cornetta, K., Morgan, R.A., and Anderson, W.F., 1991, Safety issues related to retroviral-mediated gene transfer in humans, Hum. Gene Ther. 2:5–14.
Cosset, F.-C, Takeuchi, Y., Battini, J.-L., Weiss, R.A., and Collins, M.K.L., 1995, High-titer packaging cells producing recombinant retroviruses resistant to human serum, J. Virol. 69:7430–7436.
Culver, K.W., 1994, Clinical applications of gene therapy for cancer, Clin. Chem. 40:510–512.
Culver, K.W., Ram, Z., Wallbridge, S., Ishii, H., Oldfield, E.H., and Blaese, R.M., 1992, In vivo gene transfer with retroviral vector-producer cells for treatment of experimental brain tumors, Science 256:1550–1552.
Dalmasso. A.P., Vercellotti, G.M., Fischel. R.J., Bolman. R.M., Bach. F.H., and Platt. J.L., 1992. Mechanism of complement activation in the hyperacute rejection of porcine organs transplanted into primate recipients. Am. J. Paihnl. 140:1 157–1168.
Donahue, R.E., Kessler. S.W., Bodine. D., Goodman. S., Agncola. B., Byrne. E., Raffeld, M., Moen. R., Bacher, J., Zsebo. K.M., and Nienhuis. A.W., 1992. Helper virus induced T cell Lymphoma in nonhuman primates after retroviral mediated gene transfer. J. Exp. Med. 176:1125–1135.
Famulari, N.G., 1983, Murine leukemia viruses with recombinam env genes: a discussion of their role in leukemogenesis. Curr. Top. Microbiol. Immunol. 103:103–108.
Ferry, N., Duplessis. O., Houssin. D., Danos. O., and Heard, J.-M., 1991. Retroviral-mediated gene transfer into hepatocytes in vivo. Proc. Nail. Acad. Sci. USA 88:8377–8381.
Galili, U., 1993a, Evolution and pathophysiology of the human natural anti-α-galactosyl IgG (anti-Gal) antibody. Springer Semin. Immunopathol. 15:155–171.
Galili, U., 1993b. Interaction of the natural anti-Gal antibody with α-galactosyl epitopes: a major obstacle for xenotransplantation in humans. Immunol. Today 14:480–482.
Galili, U. and Andrews. P., 1995. Suppression of α-galactosyl epitopes synthesis and production of the natural anti-gal antibody: a major evolutionary event in ancestral Old World primates. J. Hum. Evol. 29:433–443.
Galili, U., and Swanson, K., 1991. Gene sequences suggest inactivation of α1,3galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc. Satl. Acad. Sci. USA 88:7401–7404.
Galili, U., Rachmilewitz, E.A., Peleg, A., and Flechner. I., 1984, A unique natural human IgG antibody with anti-α-galactosyl specificity.J. Exp. Med. 160:1519–1531.
Galili, U., Macher, B.A., Buehler, J., and Shohet, S.B., 1985. Human natural anti-α-galactosyl IgG. II. The specific recognition of α(1–3)-linked galactose residues. J. Exp. Med. 162:573–582.
Galili. U., Clark, M.R., Shohet. S.B., Buehler, J., and Macher, B.A., 1987. Evolutionary relationship between the natural anti-Gal antibody and the Galα1–3Gal epitope in primates. Proc. Satl. Acad. Sci. USA 84:1369–1373.
Galili, U., Shohet, S.B., Kobrin. E., Stults. C.L.M., and Macher. B.A., 1988a. Man, apes, and Old World monkeys differ from other mammals in the expression of α-galactosyl epitopes on nucleated cells, J. Biol. Chem. 263:17755–17762.
Galili, U., Mandrell, R.E., Hamadeh. RM. Shohet. S.B., and Griffis. J.M., 1988b, Interaction between human natural anti-agalactosyl immunoglobulin G and bacteria of the human flora. Infect. Immun. 56:1730–1737.
Galili, U., Repik, P.M., Anaraki, F., Mozdzanowska, K., Washko, C. and Gerhard. W., 1996, Enhancement of antigen presentation of influenza virus hemagglutinin by the natural human anti-Gal antibody. Vaccine 256:160–178.
Galili, U., La Temple. D.C.and Radic. M.Z., 1998. A sensitive assay for measuring α-gal epitope expression by a monoclonal anti-Gal antibody. Transplantation 65:1129–1132.
Geyer, R., Geyer, H., Stirm, S., Hensmann, C. Schneider, J., Dabrowski, U., and Dabrowski, J., 1984, Major oligosaccharides in the glycoprotein of Friend murine leukemia virus: structure elucidation by one-and two-dimensional proton nuclear magnetic resonance and methylation analysis. Biochem. 23:5628–5637.
Goochee, CF., Gramer, M.J., Andersen, D.C., Baher, J.B., and Rasmussen, J.R., 1991, The oligosaccharides of glycoproteins: bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties. Biotechnology 9:1347–1355.
Hamadeh, R.M., Jarvis, C.A., Galili, U., Mandrell, R.E., Zhou. P., and Griffiss, J.M., 1992, Human natural anti-Gal IgG regulates alternative complement pathway activation on bacterial surfaces, J. Clin. Invest. 89:1223–1235.
Hamadeh, R.M., Galili, U., Zhou, P., and Griffis, J.M., 1995a, Anti-α-galactosyl immunoglobulin A (IgA), IgG and IgM in human secretions. Clin. Diagnos. Lab. Immunol. 2:125–131.
Hamadeh, R.M., Estabrook, M.M., Zhou, P., Jarvis, G.A., and Griffiss, J.M., 1995b, Anti-gal binds to pili of Neisseria meningitidis: the immunoglobulin A isotype blocks complement-mediated killing, Infect. Immun. 63:4900–4906.
Hatzoglou, M., Lamers, W., Bosch, F., Wynshaw-Boris, A., Clapp, D.W., and Hanson, R.W., 1990, Hepatic gene transfer in animals using retroviruses containing the promoter from the gene for phosphoenolpyruvate carboxykinase, J. Biol. Chem. 265:17285–17293.
Hoshino, H., Tanaka, H., Miwa, M., and Okada, H., 1984, Human T-cell leukemia virus is not lysed by human serum, Nature 310:324–325.
Hsieh, P., Rosner, M.R., and Robbins, P.W., 1983. Host-dependent variation of asparagine-linked oligosaccharides at individual glycosylation sites of Sindbis virus glycoproteins, J. Biol. Chem. 258:2548–2554.
Jensen, F.C., Girardi, A.J., Gilden, R.V., and Koprowski, H., 1964, Infection of human and simian tissue cultures with Rous sarcoma virus, Proc. Natl. Acad. Sci. USA 52:53–57.
Jolly, D., 1994, Viral vector systems for gene therapy, Cancer Gene Ther. 1:51–64.
Joziasse, D.H., Shaper, J.H., Van den Eijnden, D.H., Van Tunen, A.J., and Shaper, N.L., 1989, Bovine α1–3-galactosyltransferase: isolation and characterization of a cDNA clone, J. Biol. Chem. 264:14290–14297.
Kiel, W., Geyer, R., Dabrowski, J., Dabrowski, U., Niemann, H., Strim. S., and Klenk, H.-D., 1985, Carbohydrates of influenza virus. Structure elucidation of the individual glycans of the hemagglutinin by two-dimensional H NMR, and methylation analysis, EMBOJ. 4:2711–2720.
Klenk, H.-D., 1990, II. Influence of Glycosylation on Antigenicity of Viral Proteins, in: Immunochemistry of Viruses (M.H.V. van Regemortel, and A.R. Neurath, eds.), Elsevier Science Publications, New York, pp. 25–37.
Klenk, H.-D. and Rott, R., 1980, Cotranslational and posttranslational processing of viral glycoproteins, Curr. Top. Microbiol. Immunol. 90:19–48.
Kornfeld, R. and Kornfeld, S., 1976, Comparative aspects of glycosylation structure, Ann. Rev. Biochem. 45:217–237.
Kornfeld, R. and Kornfeld, S., 1985, Assembly of asparagine-linked oligosaccharides, Ann. Rev. Biochem. 54:631–664.
Larsen, R.D., Riverα-Marrero, C.A., Ernst, L.K., Cummings. R.D., and Lowe, J.B., 1990a, Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal β-D-Gal(l,4)-D-GlcNAc α(1,3)galactosyltransferasecDNA, J. Biol. Chem. 265:7055–7062.
Larsen, R.D., Ernst, L.K., Nair, R.P., and Lowe, J.B., 1990b, Molecular cloning, sequence, and expression of a human GDP-L-fucose:β-D-galactoside 2-α-L-fucosyltransferase cDN A that can form the H blood group antigen, Proc. Natl. Acad. Sci. USA 87:6674–6678.
La Temple, D.C., and Galili, U., 1998, Adult and neonatal anti-Gal response in knock-out mice for α,3galactosyltransferase, Xenotransplantation (in press).
Lemischka, I.R., Raulet, D.H., and Mulligan, R.C., 1986, Developmental potential and dynamic behavior of hematopoietic stem cells. Clin. Diagnos. Lab. Immunol. 45:917–927.
Lower, J., Davidson, E.A., Teich, N.M., Weiss, R.A., Joseph, A.P., and Kurth, R., 1981, Hetrophil human antibodies recognize oncovirus envelope antigens: epidemiological parameters and immunological specificity of the reaction, Virol. 109:409–417.
Marschang, P., Sodroski, J., Wurzner, R., and Dierich, M.P., 1995, Decay-accelerating factor (CD55) protects human immunodeficiency virus type 1 from inactivation by human complement, Eur. J. Immunol. 25:285–290.
Miller, A.D., 1992, Human gene therapy comes of age. Nature 357:455–460.
Miller, A.D. and Rosman, G.J., 1989, Improved retroviral vectors for gene transfer and expression, Biotechniques 7:980–990.
Moorman, D.W., Butler. D.A., Stanley. J.D., Lamsam. J.L., Ackermann. M.R., Jacobson. C.D., and Culver, K.W., 1994. Survival and toxicity of xenogeneic murine retroviral vector producer cells in liver. J. Surg. Oncol. 57:152–156.
Morris, C.D., 1988, Eastern Equine Encephalomyelitis. in: The Arhoviruses: Epidemiology and Ecology (T.P. Month, ed.). CRC Press. Boca Raton, pp. 1–20.
Muller-Eberhard. H.J., 1988, Molecular organization and function of the complement system. Ann. Rev Biochem. 57:321–347.
Naldini, L., Blomer, U., Gallay, P., Ory. D., Mulligan, R., Gage. F.H., Verma. I.M., and Trono. D., 1996, In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272:263–267.
Neethling. F.A., Koren. E., Ye. Y., Richards. S.V., Kujundzic. M., Oriol, R., and Cooper. D.K.C., 1994, Protection of pig kidney (PK15) cells from the cytotoxic effect of anti-pig antibodies by α-galactosyl oligosaccharides. Transplantation 57:959–963.
Oldfield. E.H. and Ram. Z., 1995. Intrathecal gene therapy for the treatment of leptomeningeal carcinomatosis. Hum. Gene Ther. 6:55–85.
Oldfield, E.H., Ram, Z., Culver, K.W., Blaese, R.M., and DeVroom. H.L., 1993. Gene therapy for the treatment of brain tumors using intrα-tumoral transduction with the thymidine kinase gene and intravenous ganciclovir, Hum. Gene Ther. 4:39–69.
Platt, J.L., Vercellotti, G.M., Dalmasso, A.P., Matas. A.J., Bolman, R.M., Najarian, J.S., and Bach, F.H., 1990, Transplantation of discordant xenografts: a review of progress. Immunol. Today 11:456–457.
Rademacher, T.W., Parekh, R.B., and Dwek. R.A., 1988, Glycobiology, Ann. Rev. Biochem. 57:785–838.
Raffel, C., Culver, K., Kohn. D., Nelson, M., Siegel, S., Gillis, F., Link. C.J., and Villablanca. J.G., 1994, Gene therapy for the treatment of recurrent pediatric malignant astrocytomas with in vivo tumor transduction with the herpes simplex thymidine kinase gene/ganciclovir system. Hum. Gene Ther. 5:863–890.
Ram, Z., Culver, K.W., Walbridge, S., Blaese, R.M., and Oldfield, E.H., 1993a, In situ retroviral-mediated gene transfer for the treatment of brain tumors in rats, Cancer Res. 53:83–88.
Ram, Z., Culver, K.W., Walbridge. S., Frank. J.A., Blaese, R.M., and Oldfield, E.H., 1993b, Toxicity studies of retroviral-mediated gene transfer for the treatment of brain tumors, J. Neurosurg. 79:400–407.
Ram, Z., Walbridge, S., Heiss. J.D., Culver, K.W., Blaese, R.M., and Oldfield, E.H., 1994a, In vivo transfer of the human interleukin-2 gene: negative tumoricidal results in experimental brain tumors, J. Neurosurg. 80:535–540.
Ram, Z., Walbridge, S., Oshiro, E.M., Viola. J.J., Chiang, Y., Mueller, S.N., Blaese. R.M., and Oldfield, E.H., 1994b. Intrathecal gene therapy for malignant leptomeningeal neoplasia. Cancer Res. 54:2141–2145.
Ram, Z., Walbridge, S., Shawker. T., Culver. K.W., Blaese, R.M., and Oldfield. E.H., 1994c, The effect of thymidine kinase transduction and ganciclovir therapy on tumor vasculature and growth of 9L gliomas in rats, J. Neurosurg. 81:256–260.
Reed, D.J., Lin, X., Thomas, T.D., Birks, C.W., Tang, J., and Rother, R.P., 1997, Alteration of glycosylation renders HIV sensitive to inactivation by normal human serum, J. Immunol. 159:4356–4361.
Repik, P.M., Strizki, J.M., and Galili, U., 1994, Differential host-dependent expression of α-galactosyl epitopes on viral glycoproteins: a study of eastern equine encephalitis virus as a model, J. Gen. Virol. 75:1177–1181.
Rettinger, S.D., Ponder. K.P., Saylors, R.L., Dennedy, S.C, Hafenrichter, D.G., and Flye, M.W., 1993, In vivo hepatocyte transduction with retrovirus during in-flow occlusion, J. Surg. Res. 54:418–425.
Rettinger, S.D., Kennedy, S.C., Wu, X., Saylors, R.L., Hafenrichter, D.G., Flye, M.W., and Ponder, K.P., 1994, Liver-directed gene therapy: quantitative evaluation of promoter elements by using in vivo retroviral transduction, Proc. Natl. Acad. Sci. USA 91:1460–1464.
Rollins, S.A., Birks, C.W., Setter, E., Squinto, S.P., and Rother, R.P., 1996, Retroviral vector producer cell killing in human serum is mediated by natural antibody and complement: strategies for evading the humoral immune system. Hum. Gene Ther. 7:619–626.
Rother, R.P. and Squinto, S.P., 1996, The α-galactosyl epitope: a sugar coating that makes viruses and cells unpalatable, Cell 86:185–188.
Rother, R.P., Fodor, W.L., Springhorn, J.P., Birks. C.W., Setter, E., Sandrin, M.S., Squinto, S.P., and Rollins, S.A., 1995a, A novel mechanism of retrovirus inactivation in human serum mediated by anti-αgalactosyl natural antibody, J. Exp. Med. 182:1345–1355.
Rother, R.P., Squinto, S.P., Mason, J.M., and Rollins, S.A., 1995b, Protection of retroviral vector particles in human blood through complement inhibition, Hum. Gene Ther. 6:429–435.
Russell, D.W., Berger, M.S., and Miller, A.D., 1995, The effects of human serum and cerebrospinal fluid on retroviral vectors and packaging cell lines, Hum. Gene Ther. 6:635–641.
Saifuddin, M., Parker, C.J., Peeples, M.E., Gorny. M.K., Zollα-Pazner, S., Ghassemi, M., Rooney, I.A., Atkinson, J.P., and Spear, G.T., 1995, Role of virion-associated glycosylphosphatidylinositol-linked proteins CD55 and CD59 in complement resistance of cell line-derived and primary isolates of HIV-1, J. Exp. Med. 182:501–509.
Sandrin, M.S., Vaughan, H.A., Dabkowski, P.L., and McKenzie. I.F.C., 1993, Anti-pig IgM antibodies in human serum react predominantly with gal(α1–3)gal epitopes, Proc. Natl. Acad. Sci. USA 90:11391–11395.
Sandrin, M.S., Fodor, W.L., Mouhtouris, E., Osman, N., Cohney, S., Rollins, S.A., Guilmette, E.R., Setter, E., Squinto, S.P., and McKenzie. I.F.C., 1995, Enzymatic remodelling of the carbohydrate surface of a xenogenic cell substantially reduces human antibody binding and complement-mediated cytolysis. Nature Med. 1:1261–1267.
Santer. U.V., DeSantis, R., Hard, K.J., van Kuik. J.A., Vliegenthart, J.F.G., Won, B., and Glick. M.C., 1989, N-linked oligosaccharide changes with oncogenic transformation require sialylation of multiantennae, Eur. J. Biochem. 181:249–260.
Schlesinger, M.J. and Schlesinger. S., 1987a. Formation and assembly of alphavirus glycoproteins, in: The Togaviridae and Flaviviridae (S. Schlesinger. and M. J. Schlesinger. eds.). Plenum Press. New York. pp. 121–148.
Schlesinger, M.J. and Schlesinger, S., 1987b. Domains of virus glycoproteins. Advances in Virus Research 33:1–44.
Schulze, I.T., 1970, The structure of influenza virus. I. The polypeptides of the virion, Virol. 41:890–904.
Smith, D.F., Larsen, R.D., Mattox, S., Lowe, J.B., and Cummings, R.D., 1990. Transfer and expression of a murine UDP-Gal:β-D-Gal-α1,3-galactosyltransferase gene in transfected Chinese hamster ovary cells, J. Biol. Chem. 265:6225–6234.
Snyder, H.W., Jr. and Fleissner, E., 1980. Specificity of human antibodies to oncovirus glycoproteins: recognition of antigen by natural antibodies directed against carbohydrate structures. Proc. Natl. Acad. Sci. USA 77:1622–1626.
Spear, G.T., Lurain, N.S., Parker, C.J., Ghassemi. M., Payne, G.H., and Saifuddin, M., 1995. Host cell-derived complement control proteins CD55 and CD59 are incorporated into the virions of two unrelated enveloped viruses, J. Immunol. 155:4376–4381.
Stollar, V., Stollar, B.D., Koo, K., Harrap. K.A., and Schlesinger, W.R., 1976, Sialic acid contents of Sindbis virus from vertebrate and mosquito cells: equivalence of biological and immunological viral properties, Virol. 69:104–115.
Strauss, J.H., Burge, B.W., and Darnell, J.E., 1970, Carbohydrate content of the membrane protein of Sindbis virus, J. Mol. Biol. 47:437–448.
Strauss, J.H. and Strauss, E.G., 1977, Togaviruses, in: The Molecular Biology of Animal Viruses (D.P. Nayak, ed.), Marcel Dekker, New York, pp. 111–166.
Takamiya, Y., Short, M.P., Moolten, F.L., Fleet, C., Mineta, T., Breakefield, X.O., and Martuza, R.L., 1993, An experimental model of retrovirus gene therapy for malignant brain tumors, J. Neurosurg. 79:104–110.
Takeuchi, Y., Cosset, F.-L., Lachmann. P.J., Okada. H., Weiss. R.A., and Collins, M.K.L., 1994, Type C retrovirus inactivation by human complement is determined by both the viral genome and the producer cell, J. Virol. 68:8001–8007.
Takeuchi, Y., Porter, C.D., Strahan, K.M., Preece. A.F., Gustafsson, K., Cosset, J.-L., Weiss, R.A., and Collins, M.K.L., 1996, Sensitization of cells and retroviruses to human serum by (α1–3) galactosyltransferase. Nature 379:85–88.
Teich, N.M., Weiss, R.A., Salahuddin. S.Z., Gallagher. R.E., Gillespie. D.H., and Gallo, R.C., 1975, Infective transmission and characterization of a C-type virus released by cultured human myeloid leukemia cells, Nature 256:551–555.
Thall, A.D., Maly, P., and Lowe, J.B., 1995. Oocyte Galα1,3Gal epitopes implicated in sperm adhesion to the zona pellucida glycoprotein ZP3 are not required for fertilization in the mouse. J. Biol. Chem. 270:21437–21440.
Thiry, L., Cogniaux-Le Clerc. J., Content. J., and Tack. L., 1978, Factors which influence inactivation of vesicular stomatitis virus by fresh human serum. Virol. 87:384–393.
Tsichlis. P.N., 1987, Oncogenesis by Moloney murine leukemia virus. Anticancer Res. 7:171–180.
Tsichlis, P.N. and Lazo. P.A., 1991. Virus-host interactions and the pathogenesis of murine and human oncogene retroviruses. Curr. Top. Microbiol. Immunol. 171:95–171.
Vaughan, H.A., Loveland. B.E., and Sandrin. M.S., 1994. Galα( 1.3)gal is the major xenoepitope expressed on pig endothelial cells recognized by naturally occurring cytotoxic human antibodies, Transplantation 58:879–882.
Welsh, R.M., Jr., 1977, Host cell modification of lymphocytic choriomeningitis virus and Newcastle disease virus altering viral inactivation by human complement, J. Immunol. 118:348–354.
Welsh, R.M., Jr., Cooper, N.R., Jensen. F.C., and Oldstone. M.B.A., 1975. Human serum lyses RNA tumour viruses. Nature 257:612–614.
Welsh, R.M., Jr., Lampert, P.W., Burner. P.A., and Oldstone. M.B.A., 1976. Antibody-complement interactions with purified lymphocytic choriomeningitis virus. Virol. 73:59–71.
Welsh, R.M., Jr., O’Donnell. C.L., Reed, D.J., and Rother, R.P., 1998, Evaluation of the galα1–3gal epitope as a host modification factor eliciting natural humoral immunity to enveloped viruses, J. Virol. (in press).
Williams, D.A., Lemischka, I.R., Nathan, D.G., and Mulligan. R.C., 1984, Introduction of a new genetic material into pluripotent haematopoietic stem cells of the mouse. Nature 310:476–480.
Wood, C., Kabat, E.A., Murphy. L.A., and Goldstein, I.J., 1979, Immunochemical studies on the combining sites of two isolectins A4 and B4 isolated from Bandeiraea simplicifolia. Arch. Biochem. Biophys. 198:1–9.
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Rother, R.P., Galili, U. (1999). α-Gal Epitopes on Viral Glycoproteins. In: Galili, U., Avila, J.L. (eds) α-Gal and Anti-Gal. Subcellular Biochemistry, vol 32. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4771-6_7
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