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Production of recombinant xenotransplantation antigen in Escherichia coli.

Abstract：

:The synthesis of sufficient amounts of oligosaccharides is the bottleneck for the study of their biological function and their possible use as drug. As an alternative for chemical synthesis, we propose to use Escherichia coli as a "living factory." We have addressed the production of the Galp alpha(1-3)Galp beta(1-4)GlcNAc epitope, the major porcine antigen responsible for xenograft rejection. An E. coli strain was generated which simultaneously expresses NodC (to provide the chitin-pentaose acceptor), beta(1-4) galactosyltransferase LgtB, and bovine alpha(1-3) galactosyltransferase GstA. This strain produced 0.68 g/L of the heptasaccharide Galp alpha(1-3)Galp beta(1-4)(GlcNAc)(5), which harbours the xenoantigen at its non-reducing end, establishing the feasibility of this approach.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bettler E,Imberty A,Priem B,Chazalet V,Heyraud A,Joziasse DH,Geremia RA

doi

10.1016/s0006-291x(03)00227-4

subject

Has Abstract

pub_date

2003-03-14 00:00:00

pages

620-4

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X03002274

journal_volume

302

pub_type

杂志文章

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