Glycobiology Advance Access originally published online on November 26, 2002
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Glycobiology, 2003, Vol. 13, No. 3 179-189
© 2003 Oxford University Press
Glycosylation of human recombinant gonadotrophins: characterization and batch-to-batch consistency
2 Laboratoires Serono Sa, Serono Biotech Center, Zone Industrielle B, CH-1809 Fenil-Sur-corsier, Switzerland
3 Laboratoire de Spectrométrie de Masse Bio-Organique, ECPM, UMR CNRS 7509, Université Louis Pasteur, 25 rue Becquerel, 67087 Strasbourg Cedex, France
Received on June 28, 2002; revised on September 20, 2002; accepted on September 23, 2002
The glycan moiety of human recombinant gonadotrophins (r-hFSH, r-hLH, and r-hCG) produced in CHO cell lines has been characterized by a combination of chromatographic and mass spectrometric techniques, including both matrix-assisted laser desorption ionization and electrospray. Two glycan mapping methods have been developed for the three gonadotrophins that allow separation of the glycans according to either their charge or sialylation level or their antennarity. A method was also developed for r-hCG that permits the complete resolution of the N-glycan from the O-glycan species. Whereas the structure found for the N-glycans of the gonadotrophins was in agreement with the complex type model, the structure for an O-glycan of r-hCG, not yet described, has been unambiguously determined using nanoelectrospray ion trap mass spectrometry. Using these two glycan mapping methods, the high level of batch-to-batch consistency achieved for the glycosylation of the three recombinant gonadotrophins in commercial production has been shown. These data demonstrate the tight control that can be achieved in the manufacturing of complex recombinant therapeutic glycoproteins, which is a prerequisite to the delivering of a guaranteed dose of drug from vial to vial, and in turn to ensuring the clinical efficacy of the product.
1 To whom correspondence should be addressed; e-mail: annick.gervais{at}serono.com
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