Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-3-4
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Epitopes, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/GstA protein, bacteria, http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/N-Acetyllactosamine Synthase, http://linkedlifedata.com/resource/pubmed/chemical/NodC protein, Rhizobiales, http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trisaccharides, http://linkedlifedata.com/resource/pubmed/chemical/alpha-galactosyl epitope
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
302
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
620-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12615080-Animals, pubmed-meshheading:12615080-Antigens, pubmed-meshheading:12615080-Bacterial Proteins, pubmed-meshheading:12615080-Carrier Proteins, pubmed-meshheading:12615080-Cattle, pubmed-meshheading:12615080-Chromatography, pubmed-meshheading:12615080-Epitopes, pubmed-meshheading:12615080-Escherichia coli, pubmed-meshheading:12615080-Escherichia coli Proteins, pubmed-meshheading:12615080-Gene Transfer Techniques, pubmed-meshheading:12615080-Glycosyltransferases, pubmed-meshheading:12615080-Models, Biological, pubmed-meshheading:12615080-N-Acetylglucosaminyltransferases, pubmed-meshheading:12615080-N-Acetyllactosamine Synthase, pubmed-meshheading:12615080-Plasmids, pubmed-meshheading:12615080-Polysaccharides, pubmed-meshheading:12615080-Recombinant Proteins, pubmed-meshheading:12615080-Swine, pubmed-meshheading:12615080-Temperature, pubmed-meshheading:12615080-Time Factors, pubmed-meshheading:12615080-Transplantation, Heterologous, pubmed-meshheading:12615080-Trisaccharides
pubmed:year
2003
pubmed:articleTitle
Production of recombinant xenotransplantation antigen in Escherichia coli.
pubmed:affiliation
Centre de Recherches sur les Macromolécules Végétales (CNRS), Affiliated with Joseph Fourier University, BP 53X, 38041 Grenoble cedex 9, France. e.bettler@cmbi.kun.nl
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't