Highly efficient chemoenzymatic synthesis of α-galactosyl epitopes with a recombinant α(1→3)-galactosyltransferase

Jianwen Fang, Jun Li, Xi Chen, Yingnan Zhang, Jianqiang Wang, Zhengmao Guo, Wei Zhang, Libing Yu, Keith Brew, Peng George Wang

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Abstract

α-Galactosyl epitopes are carbohydrate structures bearing a Galα1-3Galβ terminus. The interaction of these epitopes on the surface of animal cells with anti-α-galactosyl antibodies in human serum is believed to be the main cause in antibody-mediated hyperacute rejection in xenotransplantation. This report describes an efficient chemoenzymatic approach based on the use of recombinant α(1→3)-galactosyltransferase (α13-GalT) for the synthesis of xenoactive α-galactosyl epitopes, which are highly desired in the research of xenotransp]antation and immunotherapy. A truncated bovine α1,3-GalT (80-368) was cloned into the pET15b vector and subsequently transformed into E. coli BL21 strain. This expression system efficiently produced the soluble recombinant enzyme on a large scale with highly specific activity. A variety of α(1→3)-galactosylated epitopes were synthesized using such a recombinant enzyme. In a unique fashion, α-galactosyl pentasaccharide was synthesized via a one-pot, two-step enzymatic synthesis with in situ cofactor regeneration.

Original languageEnglish (US)
Pages (from-to)6635-6638
Number of pages4
JournalJournal of the American Chemical Society
Volume120
Issue number27
DOIs
StatePublished - Jul 15 1998
Externally publishedYes

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ASJC Scopus subject areas

  • Chemistry(all)

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