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Glycobiology Advance Access published online on November 26, 2002
Glycobiology, doi:10.1093/glycob/cwg020
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Submitted on June 28, 2002
Revised on September 20, 2002
Accepted on September 23, 2002

© 2002 Oxford University Press

ORIGINAL ARTICLES

Glycosylation of human recombinant gonadotrophins: characterisation and batch-to-batch consistency

Annick Gervais 1*, Yves-Alexis Hammel 1, Sophie Pelloux 1, Pierre Lepage 1, Gianni Baer 1, Nathalie Carte 2, Odile Sorokine 2, Jean-Marc Strub 2, Roman Koerner 2, Emmanuelle Leize 2, Alain Van Dorsselaer 2

1 Laboratoires SERONO SA, Serono Biotech Center, Zone Industrielle B, CH-1809 Fenil-Sur-Corsier, Switzerland
2 Laboratoire de Spectrométrie de Masse Bio-Organique, ECPM, UMR CNRS 7509, Université Louis Pasteur, 25 rue Becquerel, 67087 Strasbourg cedex, France

* To whom correspondence should be addressed. E-mail: annick.gervais{at}serono.com.

Abstract

The glycan moiety of human recombinant gonadotrophins (r-hFSH, r-hLH and r-hCG) produced in Chinese Hamster Ovary (CHO) cell lines has been characterised by a combination of chromatographic and mass spectrometric techniques including both Matrix-Assisted Laser Desorption Ionisation (MALDI) and electrospray (ES). Two glycan mapping methods have been developed for the three gonadotrophins that allow the separation of the glycans according to either their charge or sialylation level, or according to 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 nanoES 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 ensure the clinical efficacy of the product.


Key words: batch-to-batch consistency / glycoprotein / mass spectrometry / N-glycan structure / O-glycan structure
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