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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.

Artikel i vetenskaplig tidskrift
Författare David Smith
Roland D'Argy
Mats Nilsson
Ulf Yrlid
James de Jersey
Lars Björck
Mary Jo Wick
Publicerad i Cellular microbiology
Volym 6
Nummer/häfte 7
Sidor 609-23
ISSN 1462-5814
Publiceringsår 2004
Publicerad vid
Sidor 609-23
Språk en
Ämnesord Animals, Autoradiography, methods, B-Lymphocytes, immunology, metabolism, Bacterial Proteins, chemistry, metabolism, Binding Sites, Flow Cytometry, Iodine Radioisotopes, metabolism, Lymph Nodes, cytology, immunology, Lymphocyte Activation, immunology, Mice, Mice, Inbred C3H, Mice, Inbred C57BL, Microscopy, Confocal, Peptostreptococcus, metabolism, pathogenicity, Spleen, cytology, immunology
Ämneskategorier Medicin och Hälsovetenskap

Sammanfattning

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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