Source:http://linkedlifedata.com/resource/pubmed/id/15186398
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2004-6-9
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pubmed:abstractText |
Protein L is an immunoglobulin (Ig)-binding protein produced by the Gram-positive bacterium Peptostreptococcus magnus that interacts with the variable region of Ig kappa light chains. The Ig light chain-binding capacity of protein L gives it the potential to interact with cells expressing surface Ig such as B cells. The present study was performed to address the in vivo trafficking of protein L at both the organ and the cellular level. Using the powerful technique of whole-body autoradiography in a murine model system, we demonstrate specific targeting of protein L to secondary lymphoid tissues in whole-animal analysis. The observed targeting depends on the capacity to interact with murine Ig, as tissue targeting was not apparent in mice given protein H, an Ig-binding protein produced by Streptococcus pyogenes with affinity for human but not murine Ig. Tissue targeting data were combined with flow cytometry analysis, which demonstrated the capacity of protein L to target and activate B lymphocytes in vivo. B cells targeted by protein L had increased surface expression of CD86 and MHC-II, and protein L was present in vacuolar compartments of B cells. Protein L did not bind T cells or natural killer cells but had some capacity to target dendritic cells and macrophages. The data show that protein L preferentially targets secondary lymphoid organs, and activates and is internalized by B cells in vivo. Furthermore, the observed tissue and cell targeting properties require an affinity for murine Ig. These data support the potential use of this Ig-binding protein as a targeting approach to deliver agents to defined cell populations in vivo.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1462-5814
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
609-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15186398-Animals,
pubmed-meshheading:15186398-Autoradiography,
pubmed-meshheading:15186398-B-Lymphocytes,
pubmed-meshheading:15186398-Bacterial Proteins,
pubmed-meshheading:15186398-Binding Sites,
pubmed-meshheading:15186398-Flow Cytometry,
pubmed-meshheading:15186398-Iodine Radioisotopes,
pubmed-meshheading:15186398-Lymph Nodes,
pubmed-meshheading:15186398-Lymphocyte Activation,
pubmed-meshheading:15186398-Mice,
pubmed-meshheading:15186398-Mice, Inbred C3H,
pubmed-meshheading:15186398-Mice, Inbred C57BL,
pubmed-meshheading:15186398-Microscopy, Confocal,
pubmed-meshheading:15186398-Peptostreptococcus,
pubmed-meshheading:15186398-Spleen
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pubmed:year |
2004
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pubmed:articleTitle |
Whole-body autoradiography reveals that the Peptostreptococcus magnus immunoglobulin-binding domains of protein L preferentially target B lymphocytes in the spleen and lymph nodes in vivo.
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pubmed:affiliation |
Section for Immunology, Department of Cell and Molecular Biology, Lund University, Lund, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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