|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1993-3-23
|
|
pubmed:abstractText |
The Escherichia coli maltose-binding protein is a highly versatile carrier protein allowing the construction of genetically engineered hybrid proteins. It accepts large fusions to both C- and N-termini as well as the insertion of shorter peptides at 'permissive sites' within the continuity of the protein. We have genetically inserted immunogenic peptides corresponding to defined viral B- and T-cell epitopes into two permissive sites: one at amino acid site 133, the other at site 303. The hybrid proteins are easily purifiable and immunogenic, inducing peptide-specific B- and T-cell responses. When delivered by live bacteria (E. coli K12 and aroA Salmonella typhimurium) antibody responses can be induced against both the MalE carrier and the inserted B-cell epitope. We discuss the induction of T-cell responses by bacterial delivery systems.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
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/MalE protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Periplasmic Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vaccines, Synthetic,
http://linkedlifedata.com/resource/pubmed/chemical/maltose transport system, E coli
|
|
pubmed:status |
MEDLINE
|
|
pubmed:issn |
0264-410X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
11
|
|
pubmed:geneSymbol |
aroA
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
140-2
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:7679863-ATP-Binding Cassette Transporters,
pubmed-meshheading:7679863-Animals,
pubmed-meshheading:7679863-Antibodies, Bacterial,
pubmed-meshheading:7679863-Antigens, Bacterial,
pubmed-meshheading:7679863-B-Lymphocytes,
pubmed-meshheading:7679863-Bacterial Proteins,
pubmed-meshheading:7679863-Carrier Proteins,
pubmed-meshheading:7679863-Epitopes,
pubmed-meshheading:7679863-Escherichia coli,
pubmed-meshheading:7679863-Escherichia coli Proteins,
pubmed-meshheading:7679863-Maltose-Binding Proteins,
pubmed-meshheading:7679863-Mice,
pubmed-meshheading:7679863-Monosaccharide Transport Proteins,
pubmed-meshheading:7679863-Peptide Fragments,
pubmed-meshheading:7679863-Periplasmic Binding Proteins,
pubmed-meshheading:7679863-Protein Engineering,
pubmed-meshheading:7679863-Recombinant Fusion Proteins,
pubmed-meshheading:7679863-Salmonella typhimurium,
pubmed-meshheading:7679863-T-Lymphocytes,
pubmed-meshheading:7679863-Vaccines, Synthetic
|
|
pubmed:year |
1993
|
|
pubmed:articleTitle |
Immune responses to hybrid maltose-binding proteins.
|
|
pubmed:affiliation |
Programmation Moléculaire et Toxicologie Génétique (CNRS URA 1444), Paris, France.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
