Document Detail

Glycan engineering of proteins with whole living yeast cells expressing rat liver alpha2,3-sialytransferase in the porous cell wall.
MedLine Citation:
PMID:  9883879     Owner:  NLM     Status:  MEDLINE    
The N-glycans of recombinant proteins produced via the secretory pathway of cultured mammalian cells are often undersialylated, and insect cells lack sialytransferases. Undersialylated glycoproteins are rapidly cleared from the circulation, compromising the effect of pharmaceuticals. We show that incubation with living Saccharomyces cerevisiae cells expressing the catalytic ectodomain of rat liver alpha2,3-sialyltransferase (ST3Ne) in the porous cell wall resulted in sialylation of glycoproteins. The Km values of the yeast enzyme for several substrates were similar to those of recombinant ST3Ne from insect cells and of authentic ST3N. The yeast strain provides an inexpensive self-perpetuating source of ST3N activity for glycan engineering of recombinant proteins.
E Sievi; J Helin; R Heikinheimo; M Makarow
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  441     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1998 Dec 
Date Detail:
Created Date:  1999-01-22     Completed Date:  1999-01-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  177-80     Citation Subset:  IM    
Institute of Biotechnology, University of Helsinki, Finland.
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MeSH Terms
Asialoglycoproteins / chemistry
Catalytic Domain
Cell Wall / enzymology*
Liver / enzymology*
N-Acetylneuraminic Acid / chemistry
Polysaccharides / chemistry*
Protein Engineering*
Recombinant Proteins / chemistry,  metabolism
Saccharomyces cerevisiae / chemistry*
Sialyltransferases / chemistry*,  metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Reg. No./Substance:
0/Asialoglycoproteins; 0/Polysaccharides; 0/Recombinant Proteins; 131-48-6/N-Acetylneuraminic Acid; EC 2.4.99.-/Sialyltransferases; EC alpha-2,3-sialyltransferase

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