Quantitative control of sialylation

US9809835B2 · kind B2 · utility

Assignee

• Roche Diagnostics Operations, Inc. · US

Inventors

• Alfred Engel · Tutzing, DE
• Michael Greif · Penzberg, DE
• Christine Jung · Iffeldorf, DE
• Sebastian Malik · Antdorf, DE
• Rainer Mueller · Penzberg, DE
• Harald Sobek · Penzberg, DE
• Bernhard Suppmann · Weilheim, DE
• Marco Thomann · Beuerberg, DE

Key dates

• Filing date: Nov 24, 2015
• Grant date: Nov 7, 2017
• Expiry date: Jul 20, 2036

Classification

• Technology area (CPC C): Chemistry; Metallurgy
• CPC primary: C12P21/005
• WIPO field: Biotechnology
• WIPO sector: Chemistry

Abstract

The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations were found to exhibit sialidase enzymatic activity, particularly a variant of human sialyltransferase (hST6Gal-I) with a truncation deletion involving the first 89 N-terminal amino acids of the respective wild-type polypeptide. A fundamental finding documented in the present disclosure is that there exists a variant of this enzyme which is capable of catalyzing transfer of a glycosyl moiety as well as hydrolysis thereof. Thus, disclosed is a specific exemplary variant of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variant of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.