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PMID: 6320186 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Chimeric influenza virus hemagglutinin containing either the NH2 terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 81 ·No. 2 ·1984-01-00 ·Pages 395-9

McQueen NL, Nayak DP, Jones LV, Compans RW

Abstract

Chimeric cDNA clones of influenza virus hemagglutinin (HA) were constructed in which the DNA encoding either the NH2 terminus or the COOH terminus of HA was replaced with that of a vesicular stomatitis virus G protein. The chimeric cDNAs (GHA or HAG) were expressed in CV1 cells using the simian virus 40 late replacement promoter. Both chimeric proteins are synthesized, glycosylated, and transported to the rough endoplasmic reticulum. These results show that the NH2-terminal sequences of vesicular stomatitis virus G protein can provide a signal function for translocation and the COOH-terminal sequences can provide the anchor function for the influenza virus HA, when substituted for similar sequences. However, the chimeric glycoproteins were not transported to the Golgi complex or the plasma membrane. The implication of these results in translocation, sorting, and transport processes is discussed.

MeSH Terms
Animals Cattle Cell Compartmentation Cells, Cultured DNA, Recombinant Glycoproteins/metabolism Hemagglutinins, Viral/metabolism Influenza A virus/metabolism Membrane Glycoproteins Membrane Proteins/metabolism Structure-Activity Relationship Vesicular stomatitis Indiana virus/metabolism Viral Envelope Proteins Viral Proteins/genetics,metabolism
Chemicals
DNA, Recombinant G protein, vesicular stomatitis virus Glycoproteins Hemagglutinins, Viral Membrane Glycoproteins Membrane Proteins Viral Envelope Proteins Viral Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
McQueen N L
Nayak D P
Jones L V
Compans R W
References (23)
23 references, click to expand
  1. An Escherichia coli mutant with an amino acid alteration within the signal sequence of outer membrane prolipoprotein.
    Proc Natl Acad Sci U S A. 1978 Oct;75(10):4891-5 PMID: 368803
  2. Endo-beta-N-acetylglucosaminidases acting on the carbohydrate moieties of glycoproteins. The differential specificities of the enzymes from Streptomyces griseus and Diplococcus pneumoniae.
    J Biochem. 1974 Aug;76(2):307-17 PMID: 4154323
  3. Polarity of influenza and vesicular stomatitis virus maturation in MDCK cells: lack of a requirement for glycosylation of viral glycoproteins.
    Proc Natl Acad Sci U S A. 1979 Dec;76(12):6430-4 PMID: 230510
  4. Subcellular compartmentalization of saccharide moieties in cultured normal and malignant cells.
    J Cell Biol. 1980 May;85(2):429-34 PMID: 7372714
  5. Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells.
    Cell. 1980 May;20(1):45-54 PMID: 6248236
  6. Secretion and membrane localization of proteins in Escherichia coli.
    CRC Crit Rev Biochem. 1980;7(4):339-71 PMID: 6993100
  7. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation.
    Nature. 1981 Jan 29;289(5796):373-8 PMID: 6162101
  8. Complete sequence analysis shows that the hemagglutinins of the H0 and H2 subtypes of human influenza virus are closely related.
    Virology. 1981 May;111(1):113-24 PMID: 7233828
  9. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions.
    J Virol. 1981 Aug;39(2):519-28 PMID: 6268840
  10. Expression of antigenic determinants of the hemagglutinin gene of a human influenza virus in Escherichia coli.
    Proc Natl Acad Sci U S A. 1981 Sep;78(9):5376-80 PMID: 6170982
  11. Early and late functions associated with the Golgi apparatus reside in distinct compartments.
    Proc Natl Acad Sci U S A. 1981 Dec;78(12):7453-7 PMID: 6801652
  12. Human influenza virus hemagglutinin is expressed in monkey cells using simian virus 40 vectors.
    Proc Natl Acad Sci U S A. 1982 Jan;79(2):233-7 PMID: 6281758
  13. Cell surface expression of the influenza virus hemagglutinin requires the hydrophobic carboxy-terminal sequences.
    Cell. 1982 Sep;30(2):649-56 PMID: 6814764
  14. Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells.
    Cell. 1982 Oct;30(3):753-62 PMID: 6291783
  15. Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein.
    Nature. 1982 Dec 16;300(5893):598-603 PMID: 7144911
  16. Immune response to human influenza virus hemagglutinin expressed in Escherichia coli.
    Gene. 1983 Mar;21(3):273-84 PMID: 6343189
  17. Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA.
    Cell. 1983 Jun;33(2):435-43 PMID: 6305510
  18. Active influenza virus neuraminidase is expressed in monkey cells from cDNA cloned in simian virus 40 vectors.
    Proc Natl Acad Sci U S A. 1983 Jul;80(13):3976-80 PMID: 6306656
  19. Proposal for a common oligosaccharide intermediate in the synthesis of membrane glycoproteins.
    Cell. 1977 Dec;12(4):893-900 PMID: 202393
  20. Homologous interference mediated by defective interfering influenza virus derived from a temperature-sensitive mutant of influenza virus.
    J Virol. 1978 Oct;28(1):375-86 PMID: 702654
  21. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  22. Purification and properties of an endo-beta-N-acetylglucosaminidase from Streptomyces griseus.
    J Biol Chem. 1974 Feb 10;249(3):811-7 PMID: 4204552
  23. Asymmetric budding of viruses in epithelial monlayers: a model system for study of epithelial polarity.
    Proc Natl Acad Sci U S A. 1978 Oct;75(10):5071-5 PMID: 283416
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.81.2.395
Published
1984-01-00
Pages
395-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC344683
Subset
IM
Grants
NIAID NIH HHS · R01 AI12680 · United States
NIAID NIH HHS · R01 AI16348 · United States
NIAID NIH HHS · R01 AI2749 · United States
External Links
PubMed source DOI: 10.1073/pnas.81.2.395 PMC Full Text View journal details
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