Development of antibodies to unprotected glycosylation sites on recombinant human GM-CSF.

@article{Gribben1990DevelopmentOA,
  title={Development of antibodies to unprotected glycosylation sites on recombinant human GM-CSF.},
  author={John G Gribben and Stephen Devereux and Nick S. T. Thomas and Matthias Keim and Hilton M Jones and Anthony H. Goldstone and David Christopher Linch},
  journal={Lancet},
  year={1990},
  volume={335 8687},
  pages={434-7}
}
In 4 out of 16 patients receiving recombinant human granulocyte macrophage colony stimulating factor (rhGM-CSF) in phase I/II studies antibodies developed to the recombinant protein. The antibodies react with sites on the native protein backbone which are normally protected by O-linked glycosylation but which are exposed in rhGM-CSF produced in yeast and Escherichia coli. Antigenicity of recombinant human proteins due to non glycosylation may have relevance to the choice of host system for… CONTINUE READING

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