rdf:type |
|
lifeskim:mentions |
umls-concept:C0006034,
umls-concept:C0007634,
umls-concept:C0017262,
umls-concept:C0024198,
umls-concept:C0036536,
umls-concept:C0036537,
umls-concept:C0038164,
umls-concept:C0185117,
umls-concept:C0450442,
umls-concept:C0740009,
umls-concept:C1382107,
umls-concept:C2911684
|
pubmed:issue |
3
|
pubmed:dateCreated |
2006-6-16
|
pubmed:abstractText |
The ospA gene of Borrelia burgdorferi codes for an outer membrane lipoprotein, which is a major antigen of the Lyme disease agent. Recombinant OspA vaccines tested so far were expressed in Escherichia coli. In this study, we investigated the expression of a soluble OspA protein in Nicotiana tabacum suspension cells and evaluated the secretion of OspA driven by either its own bacterial signal peptide or a plant signal peptide fused to the amino-terminal cysteine of the mature form. In both cases, the signal peptide was cleaved off and OspA secreted. During secretion, OspA was N-glycosylated. Addition of a C-terminal KDEL sequence led to retention of OspA in the endoplasmic reticulum.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0962-8819
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
15
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
325-35
|
pubmed:meshHeading |
pubmed-meshheading:16779648-Antigens, Surface,
pubmed-meshheading:16779648-Bacterial Outer Membrane Proteins,
pubmed-meshheading:16779648-Bacterial Vaccines,
pubmed-meshheading:16779648-Borrelia burgdorferi,
pubmed-meshheading:16779648-Endoplasmic Reticulum,
pubmed-meshheading:16779648-Escherichia coli,
pubmed-meshheading:16779648-Gene Expression Regulation, Plant,
pubmed-meshheading:16779648-Genetic Techniques,
pubmed-meshheading:16779648-Genetic Vectors,
pubmed-meshheading:16779648-Glycosylation,
pubmed-meshheading:16779648-Lipoproteins,
pubmed-meshheading:16779648-Models, Genetic,
pubmed-meshheading:16779648-Plant Diseases,
pubmed-meshheading:16779648-Plants, Genetically Modified,
pubmed-meshheading:16779648-Protein Processing, Post-Translational,
pubmed-meshheading:16779648-Protein Structure, Tertiary,
pubmed-meshheading:16779648-Tobacco,
pubmed-meshheading:16779648-Transgenes
|
pubmed:year |
2006
|
pubmed:articleTitle |
Expression and secretion of recombinant outer-surface protein A from the Lyme disease agent, Borrelia burgdorferi, in Nicotiana tabacum suspension cells.
|
pubmed:affiliation |
Unité de Biochimie Physiologique, Institut des Sciences de la Vie, Université catholique de Louvain, Croix du Sud 5-15, 1348, Louvain-la-Neuve, Belgium.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|