Synthetic glycobiology: exploits in the Golgi compartment

The challenge of engineering glycosylation has been confronted by synthetic chemists, biochemists and cell biologists, each with the primary goal of optimizing glycoconjugates for therapeutic applications. In nature, glycans are constructed by glycosyltransferases that are organized in an assembly l...

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Bibliographic Details
Published inCurrent opinion in chemical biology Vol. 10; no. 6; pp. 645 - 651
Main Authors Czlapinski, Jennifer L, Bertozzi, Carolyn R
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.12.2006
Subjects
Glycoproteins - biosynthesis
Glycoproteins - genetics
Golgi Apparatus - metabolism
Humans
Pichia - genetics
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
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Summary:The challenge of engineering glycosylation has been confronted by synthetic chemists, biochemists and cell biologists, each with the primary goal of optimizing glycoconjugates for therapeutic applications. In nature, glycans are constructed by glycosyltransferases that are organized in an assembly line in the endoplasmic reticulum and Golgi compartment. Recent insights into the domain architecture, localization and regulation of glycosyltransferases have provided a platform for engineering their position within the secretory pathway and access to substrates. Using this knowledge, glycosyltransferase assembly lines have been redesigned for the production of specific glycan structures using protein engineering and chemical approaches. These efforts epitomize the emerging field of ‘synthetic glycobiology’.
Bibliography:ObjectType-Article-2
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ISSN:1367-5931
1879-0402
DOI:10.1016/j.cbpa.2006.10.009