Efficient Intracellular Delivery of a Protein and a Low Molecular Weight Substance via Recombinant Polyomavirus-like Particles

Efficient encapsulation of foreign molecules like proteins and low molecular weight drugs into polyoma virus-like particles (capsoids) was achieved by the development of an anchoring technique based upon the specific interaction of the inner core protein VP2 with VP1 pentamers. A stretch of 49 amino...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 279; no. 26; pp. 27410 - 27421
Main Authors:	Abbing, Andrea, Blaschke, Ulrich K., Grein, Swen, Kretschmar, Michael, Stark, Christoph M.B., Thies, Michael J.W., Walter, Jürgen, Weigand, Martina, Woith, Diemuth C., Hess, Jürgen, Reiser, Christian O.A.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 25-06-2004 American Society for Biochemistry and Molecular Biology
Subjects:	3T3 Cells Amino Acid Sequence Animals Capsid Proteins - administration & dosage Capsid Proteins - chemistry Capsid Proteins - genetics Capsid Proteins - metabolism Capsid Proteins - pharmacokinetics Cell Survival - drug effects Drug Stability Escherichia coli - genetics Escherichia coli - virology Fluorescence Polarization Green Fluorescent Proteins Leukocytes - metabolism Luminescent Proteins - chemistry Luminescent Proteins - genetics Methotrexate - administration & dosage Methotrexate - chemistry Methotrexate - pharmacokinetics Mice Molecular Sequence Data Molecular Weight Polyomavirus - chemistry Polyomavirus - genetics Precipitin Tests Recombinant Fusion Proteins - administration & dosage Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Tumor Cells, Cultured
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Summary:	Efficient encapsulation of foreign molecules like proteins and low molecular weight drugs into polyoma virus-like particles (capsoids) was achieved by the development of an anchoring technique based upon the specific interaction of the inner core protein VP2 with VP1 pentamers. A stretch of 49 amino acids of VP2 served as an anchor molecule, either expressed as a fusion protein with green fluorescent protein (GFP) or covalently linked to methotrexate (MTX). The loaded capsoids showed regular morphology and stability for several months. GFP and MTX were internalized into cells in vitro, as was demonstrated by the detection of GFP and VP1 fluorescence in mouse fibroblasts and the cytostatic effect of intracellularly released MTX on leukemia T cells.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0021-9258 1083-351X
DOI:	10.1074/jbc.M313612200