Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
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