Polylactosaminoglycan Modification of a Small Integral Membrane Glycoprotein, Influenza B Virus NB

Literature Cited

• Bassiri, M., and M. L. Privalsky. 1986. Mutagenesis of the avian erythroblastosis virus erbB coding region: an intact extracellular domain is not required for oncogenic transformation. J. Virol. 59:525-530.
   PubMedGoogle Scholar
• Brock, C. J., M. J. A. Tanner, and C. Kempf. 1983. The human erythrocyte anion-transport protein. Biochem. J. 213:577-586.
   PubMedGoogle Scholar
• Caton, A. J., G. G. Brownlee, J. W. Yewdell, and W. Gerhard. 1982. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (Hl subtype). Cell 31:417-427.
   PubMed Web of Science ®Google Scholar
• Copeland, C. S., R. W. Donis, E. M. Bolzau, R. G. Webster, and A. Helenius. 1986. Assembly of influenza hemagglutinin trimers and its role in intracellular transport. J. Cell Biol. 103:1179-1191.
   PubMed Web of Science ®Google Scholar
• Crowley, J. F., I. J. Goldstein, J. Arnarp, and J. Lonngren. 1984. Carbohydrate binding studies on the lectin from Datura stramonium seeds. Arch. Biochem. Biophys. 231:524-533.
   PubMed Web of Science ®Google Scholar
• Cummings, R. D., and S. Komfeld. 1982. Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography. J. Biol. Chem. 257:11235-11240.
   PubMed Web of Science ®Google Scholar
• Cummings, R. D., and S. Kornfeld. 1984. The distribution of repeating [Galβ14GlcNAcβl,3] sequences in asparagine-linked oligosaccharides of the mouse lymphoma cell lines BW5147 and PHAR 2.1. J. Biol. Chem. 259:6253-6260.
   PubMed Web of Science ®Google Scholar
• Daniels, R. S., A. R. Douglas, F. Gonsalves-Scarano, G. Palu, J. J. Skehel, E. Brown, M. Knossow, I. A. Wilson, and D. C. Wiley. 1983. Antigenic structure of influenza virus haemagglutinin, p. 9-18. In W. G. Laver (ed.), The origin of pandemic influenza viruses. Elsevier Science Publishing, Inc., New York.
   Google Scholar
• Eckhardt, A. E., and I. J. Goldstein. 1983. Isolation and characterization of a family of α-D-galactosyl-containing glycopeptides from Ehrlich ascites tumor cells? Biochemistry 22:5290-5297.
   PubMedGoogle Scholar
• Elder, J. H., and S. Alexander. 1982. endo-βN-Acetylglucos-aminidase F: endoglycosidase from Flavobacterium mengingosepticum that cleaves both high-mannose and complex carbohydrates. Proc. Natl. Acad. Sci. USA 79:4540-4544.
   PubMed Web of Science ®Google Scholar
• Etchinson, J. R., and J. J. Holland. 1974. Carbohydrate composition of the membrane glycoprotein of vesicular stomatitis virus grown in four mammalian cell lines. Proc. Natl. Acad. Sci. USA 71:4011-4014.
   PubMedGoogle Scholar
• Eyler, E. H. 1965. On the biological role of glycoproteins. J. Theor. Biol. 10:89-113.
   Google Scholar
• Fukuda, M. 1985. Cell surface glycoconjugates as onco-differentiation markers in hematopoietic cells. Biochim. Biophys. Acta 780:119-150.
   PubMedGoogle Scholar
• Fukuda, M., B. Bothner, P. Ramsamooj, A. Dell, P. R. Tiller, A. Varki, and J. C. Klock. 1985. Structures of sialylated fucosyl polylactosaminoglycans isolated from chronic myelogeneous leukemia cells. J. Biol. Chem. 260:12957-12967.
   PubMedGoogle Scholar
• Fukuda, M., A. Dell, and M. N. Fukuda. 1984. Structure of fetal lactosaminoglycan. J. Biol. Chem. 259:4782-4791.
   PubMed Web of Science ®Google Scholar
• Fukuda, M., A. Dell, J. E. Oates, and M. N. Fukuda. 1984. Structure of branched lactosaminoglycan, the carbohydrate moiety of band 3 isolated from adult human erythrocytes. J. Biol. Chem. 259:8260-8273.
   PubMed Web of Science ®Google Scholar
• Fukuda, M., and M. N. Fukuda. 1984. Cell surface glycoproteins and carbohydrate antigens in development and differentiation of human erythroid cells, p. 183-234. In R. J. Ivatt (ed.), The biology of glycoproteins. Plenum Publishing Corp., New York.
   Google Scholar
• Fukuda, M., M. N. Fukuda, and S. Hakomori. 1979. Development change and genetic defect in the carbohydrate structure of band 3 glycoprotein of human erythrocyte membrane. J. Biol. Chem. 254:3700-3703.
   PubMed Web of Science ®Google Scholar
• Fukuda, M. N., M. Fukuda, and S. Hakomori. 1979. Cell surface modification by endo-β-galactosidase. J. Biol. Chem. 254:5458-5465.
   PubMedGoogle Scholar
• Gahmberg, C. G., M. Jokinen, K. K. Karhi, and L. C. Andersson. 1980. Effect of tunicamycin on the biosynthesis of the major human red cell sialoglycoprotein, glycophorin A, in the leukemia cell line K562. J. Biol. Chem. 255:2169-2175.
   PubMedGoogle Scholar
• Gething, M.-J., K. McCammon, and J. Sambrook. 1986. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell 46:939-950.
   PubMedGoogle Scholar
• Guan, J.-L., C. E. Machamer, and J. K. Rose. 1985. Glycosylation allows cell-surface transport of an anchored secretory protein. Cell 42:489-496.
   PubMedGoogle Scholar
• Hannink, M., and D. J. Donoghue. 1986. Cell surface expression of membrane-anchored v-sis gene products: glycosylation is not required for cell surface transport. J. Cell Biol. 103:2311-2322.
   PubMedGoogle Scholar
• Hannink, M., M. K. Sauer, and D. J. Donoghue. 1986. Deletions in the C terminus of the v-sis gene: dimerization is required for transformation. Mol. Cell. Biol. 6:1304-1314.
   PubMedGoogle Scholar
• Hickman, S., and S. Kornfeld. 1978. Effect of tunicamycin on IgM, IgA, and IgG secretion by mouse plasmacytoma cells. J. Immunol. 121:990-996.
   PubMed Web of Science ®Google Scholar
• Jennings, M. L., M. Adams-Lackey, and G. H. Denney. 1984. Peptides of human erythrocyte band 3 protein produced by extracellular papain cleavage. J. Biol. Chem. 259:4652-4660.
   PubMedGoogle Scholar
• Jennings, M. L., and J. S. Nicknish. 1984. Erythrocyte band 3 protein: evidence for multiple membrane-crossing segments in the 17000-dalton chymotryptic fragment? Biochemistry 23:6432-6436.
   PubMedGoogle Scholar
• Keller, R. K., and G. D. Swank. 1978. Tunicamycin does not block ovalbumin secretion in the oviduct. Biochem. Biophys. Res. Commun. 85:762-768.
   PubMed Web of Science ®Google Scholar
• Kopito, R. R., and H. F. Lodish. 1985. Primary structure and transmembrane orientation of the murine anion exchange protein. Nature (London) 316:234-238.
   PubMed Web of Science ®Google Scholar
• Kornfeld, R., and S. Kornfeld. 1980. Structure of glycoproteins and their oligosaccharide units, p. 1-34. In W. J. Lennarz (ed.), The biochemistry of glycoproteins and proteoglycans. Plenum Publishing Corp., New York.
   Google Scholar
• Kornfeld, R., and S. Kornfeld. 1985. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54:631-664.
   PubMed Web of Science ®Google Scholar
• Lamb, R. A. 1983. The influenza virus RNA segments and their encoded proteins, p. 21-69. In P. Palese and D. W. Kingsbury (ed.), Genetics of influenza viruses. Springer-Verlag KG, Vienna.
   Google Scholar
• Lamb, R. A., and P. W. Choppin. 1976. Synthesis of influenza proteins in infected cells: translation of viral polypeptides, including three P polypeptides, from RNA produced by primary transcription. Virology 74:504-519.
   PubMedGoogle Scholar
• Lamb, R. A., and P. W. Choppin. 1977. The synthesis of Sendai virus polypeptides in infected cells. III. Phosphorylation of polypeptides. Virology 81:382-397.
   PubMedGoogle Scholar
• Lamb, R. A., and P. W. Choppin. 1979. Segment 8 of the influenza virus genome is unique in coding for two polypeptides. Proc. Natl. Acad. Sci. USA 76:4908-4912.
   PubMed Web of Science ®Google Scholar
• Lamb, R. A., P. R. Etkind, and P. W. Choppin. 1978. Evidence for a ninth influenza viral polypeptide. Virology 91:60-78.
   PubMedGoogle Scholar
• Lamb, R. A., and C.-J. Lai. 1982. Spliced and unspliced messenger RNAs synthesized from cloned influenza virus M DNA in an SV40 vector: expression of the influenza virus membrane protein (MJ. Virology 123:237-256.
   PubMed Web of Science ®Google Scholar
• Lamb, R. A., S. L. Zebedee, and C. D. Richardson. 1985. Influenza virus M2 protein is an integral membrane protein expressed on the infected cell surface. Cell 40:627-633.
   PubMed Web of Science ®Google Scholar
• Li, E., R. Gibson, and S. Komfeld. 1980. Structure of an unusual complex-type oligosaccharide isolated from Chinese hamster ovary cells. Arch. Biochem. Biophys. 199:393-399.
   PubMed Web of Science ®Google Scholar
• Machamer, C. E., R. Z. Florkiewicz, and J. K. Rose. 1985. A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface. Mol. Cell. Biol. 5:3074-3083.
   PubMedGoogle Scholar
• Nakamura, K., and R. W. Compans. 1978. Effects of glucosamine, 2-deoxyglucose, and tunicamycin on glycosylation, sulfation, and assembly of influenza viral proteins. Virology 84:303-319.
   PubMed Web of Science ®Google Scholar
• Nakamura, K., and R. W. Compans. 1979. Host cell-and virus strain-dependent differences in oligosaccharides of hemagglutinin glycoproteins of influenza A viruses. Virology 95:8-23.
   PubMedGoogle Scholar
• Parekh, R. B., A. G. D. Tse, R. A. Dwek, A. F. Williams, and T. W. Rademacher. 1987. Tissue-specific N-glycosylation, sitespecific oligosaccharide patterns and lentil lectin recognition of rat Thy-1. EMBO J. 6:1233-1244.
   PubMedGoogle Scholar
• Pollack, L., and P. H. Atkinson. 1983. Correlation of glycosylation forms with position in amino acid sequence. J. Cell Biol. 97:293-300.
   PubMedGoogle Scholar
• Roth, M. G., J. P. Fitzpatrick, and R. W. Compans. 1979. Polarity of influenza and vesicular stomatitis virus maturation in MDCK cells: lack of a requirement for glycosylation of viral glycoproteins. Proc. Natl. Acad. Sci. USA 76:6430-6434.
   PubMedGoogle Scholar
• Sabban, E., V. Marchesi, M. Adesnik, and D. D. Sabatini. 1981. Erythrocyte membrane protein band 3: its synthesis and incorporation into membranes. J. Cell Biol. 91:637-646.
   PubMed Web of Science ®Google Scholar
• Schatzman, R. C., G. I. Evna, M. L. Privalsky, and J. M. Bishop. 1986. Orientation of the v-erb-B gene product in the plasma membrane. Mol. Cell. Biol. 6:1329-1333.
   PubMedGoogle Scholar
• Shaw, M. W., and P. W. Choppin. 1984. Studies on the synthesis of the influenza B virus NB glycoprotein. Virology 139:178-184.
   PubMedGoogle Scholar
• Shaw, M. W., P. W. Choppin, and R. A. Lamb. 1983. A previously unrecognized influenza B virus glycoprotein from a bicistronic mRNA that also encodes the viral neuraminidase. Proc. Natl. Acad. Sci. USA 80:4879-4883.
   PubMedGoogle Scholar
• Skehel, J. J., D. J. Stevens, R. S. Daniels, A. R. Douglas, M. Knossow, I. A. Wilson, and D. C. Wiley. 1984. A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody. Proc. Natl. Acad. Sci. USA 81:1779-1783.
   PubMed Web of Science ®Google Scholar
• Struck, D. K., P. B. Siuta, M. D. Lane, and W. J. Lennarz. 1978. Effect of tunicamycin on the secretion of serum proteins by primary cultures of rat and chick hepatocytes. J. Biol. Chem. 253:5332-5337.
   PubMed Web of Science ®Google Scholar
• Takatsuki, A., K. Kohno, and G. Ramura. 1975. Inhibition of biosynthesis of polyisoprenol sugars in chick embryo microsomes by tunicamycin. Agric. Biol. Chem. 39:2089-2091.
   Web of Science ®Google Scholar
• Tarentino, A. L., C. M. G6mez, and T. H. Plummer, Jr. 1985. Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F. Biochemistry 24:4665-4671.
   PubMed Web of Science ®Google Scholar
• Tarentino, A. L., and F. Maley. 1974. Purification and properties of an endo-p-acetylglucosaminidase from Streptomyces griseus. J. Biol. Chem. 249:811-817.
   PubMedGoogle Scholar
• von Figure, K., and A. Hasilik. 1986. Lysosomal enzymes and their receptors. Annu. Rev. Biochem. 55:167-193.
   PubMedGoogle Scholar
• Wickner, W. T., and H. F. Lodish. 1985. Multiple mechanisms of protein insertion into and across membranes. Science 230:400-407.
   PubMed Web of Science ®Google Scholar
• Wiley, D. C., I. A. Wilson, and J. J. Skehel. 1981. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature (London) 289:373-378.
   PubMed Web of Science ®Google Scholar
• Williams, M. A., and R. A. Lamb. 1986. Determination of the orientation of an integral membrane protein and sites of glycosylation by oligonucleotide-directed mutagenesis: influenza B virus NB glycoprotein lacks a cleavable signal sequence and has an extracellular NH2-terminal region? Mol. Cell. Biol. 6:4317-4328.
   PubMed Web of Science ®Google Scholar
• Winterburn, P. J., and C. F. Phelps. 1972. The significance of glycosylated proteins. Nature (London) 236:147-151.
   PubMed Web of Science ®Google Scholar
• Yamashita, K., T. Ohkura, Y. Tachibana, S. Takasaki, and A. Kobata. 1984. Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. J. Biol. Chem. 259:10834-10840.
   PubMedGoogle Scholar
• Yoshima, J., S. Takasaki, and A. Kobata. 1980. The asparagine-linked sugar chains of the glycoproteins in calf thymocyte plasma membrane. J. Biol. Chem. 255:10793-10840.
   PubMedGoogle Scholar
• Zebedee, S. L., C. D. Richardson, and R. A. Lamb. 1985. Characterization of the influenza virus M2 integral membrane protein and expression at the infected-cell surface from cloned cDNA. J. Virol. 56:502-511.
   PubMed Web of Science ®Google Scholar