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The rabies virus glycoprotein (G protein) has several important functions and is a major antigenic stimulus of the host immune system following rabies virus infection or vaccination. We developed a model system for studying the role of N-linked glycosylation in the intracellular transport and antigenicity of this molecule. The full-length cDNA of the G protein of the ERA strain of rabies virus was inserted into the eukaryotic shuttle vector pSG5 and then stably transfected into wild-type Chinese hamster ovary (CHO) cells and mutant CHO cell lines defective in glycosylation. Transfected wild-type CHO cells expressed the G protein (detected by immunofluorescence) on the cell surface in a manner similar to rabies virus-infected cells. The transfected wild-type CHO cells were shown by immunoprecipitation to produce a protein of 67K that comigrated with the fully glycosylated G protein isolated from virus-infected cells or purified virions. Treatment of the transfected cell lines with tunicamycin completely blocked surface expression and resulted in the intracellular accumulation of the G protein, suggesting that the presence of N-linked oligosaccharides is important for transport of this glycoprotein to the plasma membrane. The G protein cDNA was also expressed in the lectin-resistant CHO cell lines Lec 1, Lec 2 and Lec 8. In these cells initial N-linked glycosylation does occur, but later steps in processing of the oligosaccharides are blocked. In each case, the G protein was expressed on the surface of lectin-resistant CHO cells in a similar manner to expression on wild-type CHO cells. This suggests that various different N-linked oligosaccharide structures support intracellular transport of this glycoprotein. Thus, stably transfected CHO cell lines will provide a useful model system for further studies of the role of N-linked glycosylation in trafficking and antigenicity of the rabies virus G protein.
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
June 2011,
Sheng wu gong cheng xue bao = Chinese journal of biotechnology,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
July 1990,
Proceedings of the National Academy of Sciences of the United States of America,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
January 2016,
Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
September 1980,
Biochimica et biophysica acta,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
January 1989,
Anticancer research,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
November 2013,
Metabolic engineering,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
January 1995,
Cytotechnology,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
November 1987,
Molecular and cellular biology,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
November 1989,
Biochemical and biophysical research communications,
S R Burger, and
A T Remaley, and
J M Danley, and
J Moore, and
R J Muschel, and
W H Wunner, and
S L Spitalnik
December 1993,
Journal of virology,
