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 language | English (US) |
|---|---|
| Pages (from-to) | 6635-6638 |
| Number of pages | 4 |
| Journal | Journal of the American Chemical Society |
| Volume | 120 |
| Issue number | 27 |
| DOIs | |
| State | Published - Jul 15 1998 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Chemistry(all)
Cite this
Highly efficient chemoenzymatic synthesis of α-galactosyl epitopes with a recombinant α(1→3)-galactosyltransferase. / Fang, Jianwen; Li, Jun; Chen, Xi; Zhang, Yingnan; Wang, Jianqiang; Guo, Zhengmao; Zhang, Wei; Yu, Libing; Brew, Keith; Wang, Peng George.
In: Journal of the American Chemical Society, Vol. 120, No. 27, 15.07.1998, p. 6635-6638.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Highly efficient chemoenzymatic synthesis of α-galactosyl epitopes with a recombinant α(1→3)-galactosyltransferase
AU - Fang, Jianwen
AU - Li, Jun
AU - Chen, Xi
AU - Zhang, Yingnan
AU - Wang, Jianqiang
AU - Guo, Zhengmao
AU - Zhang, Wei
AU - Yu, Libing
AU - Brew, Keith
AU - Wang, Peng George
PY - 1998/7/15
Y1 - 1998/7/15
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0032528232&partnerID=8YFLogxK
U2 - 10.1021/ja9808898
DO - 10.1021/ja9808898
M3 - Article
AN - SCOPUS:0032528232
VL - 120
SP - 6635
EP - 6638
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 27
ER -