Abstract
The DNA sequences encoding the amino-terminal signal peptide or the carboxy-terminal hydrophobic anchor have been deleted from a cloned gene coding for the haemagglutinin (HA) of influenza virus. The wild-type gene has previously been shown to be expressed with high efficiency from simian virus 40 (SV40)-HA recombinant vectors into a fully glycosylated protein that is displayed on the infected cell's surface in an antigenically and biologically active form. The anchor-minus HA also is glycosylated but is secreted efficiently into the medium. By contrast, the signal-minus HA is produced only at low levels, is not glycosylated and is located intracellularly.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Blobel, G. et al. Symp. Soc. exp. Biol. 33, 9–36 (1979).
Davis, B. D. & Tai, P.-C. Nature 283, 433–438 (1980).
Sabatini, D. D., Kreibich, G., Morimoto, T. & Adesnik, M. J. Cell Biol. 92, 1–22 (1982).
Kreibich, G., Czako-Graham, M., Grebenan, R. C. & Sabatini, D. D. Ann. N.Y. Acad. Sci. 343, 17–33 (1980).
McCauley, J. et al. FEBS Lett. 108, 422–426 (1979).
Gething, M.-J., Bye, J. M., Skehel, J. J. & Waterfield, M. D. Nature 287, 301–306 (1980).
Tomita, M. & Marchesi, V. T. Proc. natn. Acad. Sci. U.S.A. 72, 2964–2968 (1975).
Burnstein, Y. & Schecter, I. Biochemistry 17, 2392–2400 (1978).
Springer, T. A. & Strominger, J. L. Proc. natn. Acad. Sci. U.S.A. 73, 2481–2482 (1976).
Rogers, J. et al. Cell 26, 19–27 (1981).
Porter, A. G. et al. Nature 282, 471–477 (1979).
Verhoeyen, M. et al. Nature 286, 171–776 (1980).
Both, G. W. & Sleigh, M. J. Nucleic Acids Res. 8, 2561–2575 (1980).
Min Jou, W. et al. Cell 19, 683–696 (1980).
Winter, G., Fields, S. & Brownlee, G. G. Nature 292, 72–75 (1981).
Hiti, A. L., Davis, A. R. & Nayak, D. P. Virology 111, 113–124 (1981).
Wilson, I. A., Skehel, J. J. & Wiley, D. C. Nature 289, 366–373 (1981).
Wiley, D. C., Skehel, J. J. & Waterfield, M. D. Virology 79, 446–448 (1977).
Skehel, J. J. & Waterfield, M. D. Proc. natn. Acad. Sci. U.S.A. 72, 93–97 (1975).
Wiley, D. C., Wilson, I. A. & Skehel, J. J. Nature 289, 373–378 (1981).
Hirst, G. K. J. exp. Med. 75, 49–64 (1942).
Matlin, K., Reggio, H., Helenius, A. & Simons, K. J. Cell Biol. 8, 404–420 (1981).
White, J. M., Helenius, A. & Gerthing, M.-J. Nature 300, 658–659 (1982).
Heiland, I. & Gething, M.-J. Nature 292, 851–852 (1981).
Gething, M.-J. & Sambrook, J. Nature 293, 620–625 (1981).
Gething, M.-J., Heiland, I. & Sambrook, J. in Prospective Biological Products for Viral Diseases (ed. Bachmann, P. A.) 81–89 (Taylor & Francis, London, 1981).
Gething, M.-J. & Sambrook, J. in Eukaryotic Vectors (ed. Gluzman, Y.) 29–33 (Cold Spring Harbor Laboratory, New York, 1982).
Maniatis, T., Fritsch, E. & Sambrook, J. in Molecular Cloning (Cold Spring Harbor Laboratory, New York, 1982).
Pipas, J. M., Adler, S. P., Peden, K. W. C. & Nathans, D. Cold Spring Harb. Symp. quant. Biol. 44, 285–291 (1980).
McCutchan, J. H. & Pagano, J. S. J. natn. Cancer Inst. 41, 351–357 (1968).
Hirt, B. J. molec. Biol. 26, 365–369 (1967).
Thomas, P. S. Proc. natn. Acad. Sci. U.S.A. 77, 5201–5205 (1980).
Takatsuki, A., Kohno, K. & Tamura, A. Agric. biol Chem. 39, 2089–2091 (1975).
Hubbard, S. C. & Robbins, P. W. J. biol Chem. 254, 4568–4576 (1979).
Neuberger, A., Gottschalk, A., Marshall, R. O. & Spiro, R. G. in The Glycoproteins: Their Composition, Structure and Function (ed. Gottschalk, A.) 450–490 (Elsevier, Amsterdam, 1972).
Waechter, C. J. & Lennarz, W. J. A. Rev. Biochem. 45, 95–112 (1976).
Hunt, L. A., Etchison, J. R. & Summers, D. F. Proc. natn. Acad. Sci. U.S.A. 75, 754–758 (1978).
Tabas, I. & Kornfeld, S. J. biol. Chem. 254, 11655–11663 (1979).
Tartakoff, A., Vassalli, P. & Detraz, M. J. Cell Biol. 83, 284–299 (1979).
Gething, M.-J., White, J. & Waterfield, M. Proc. natn. Acad. Sci. U.S.A. 75, 2737–2740 (1978).
Nakamura, K. & Compans, R. W. Virology 95, 8–23 (1979).
Anderson, D. J., Walter, P. & Blobel, G. J. Cell Biol. 93, 501–506 (1982).
Meyer, D. I., Krause, E. & Dobberstein, B. Nature 297, 647–650 (1982).
Strous, G. J. & Lodish, H. F. Cell 22, 709–717 (1980).
Perlman, D., Halvorson, H. O. & Cannon, E. Proc. natn. Acad. Sci. U.S.A. 79, 781–785 (1982).
Rogers, J. et al. Cell 20, 303–312 (1980).
Early, P. et al. Cell 20, 313–319 (1980).
Sveda, M. M., Markoff, L. J. & Lai, C.-J. Cell 30, 649–656 (1982).
Maxam, A. M. & Gilbert, W. Proc. natn. Acad. Sci. U.S.A. 74, 560–564 (1977).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Gething, MJ., Sambrook, J. Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein. Nature 300, 598–603 (1982). https://doi.org/10.1038/300598a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/300598a0
This article is cited by
-
C3d enhancement of antibodies to hemagglutinin accelerates protection against influenza virus challenge
Nature Immunology (2000)
-
Molecular and immunological characterization of soluble aggregated A/Victoria/3/75 (H3N2) influenza haemagglutinin expressed in insect cells
Archives of Virology (1996)
-
Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein
Nature (1990)
-
Serologic specificity of antibodies to herpes simplex virus glycoprotein B present in human sera Analysis by transient expression of glycoprotein B-derivatives
Archives of Virology (1990)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.