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J. Biol. Chem., Vol. 276, Issue 18, 15042-15050, May 4, 2001
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From the Marie Curie Research Institute, The Chart, Oxted,
Surrey RH8 0TL, United Kingdom
VP22, a structural protein of herpes simplex
virus, exhibits unusual trafficking properties which we proposed might
be exploited in gene and protein delivery applications. To pursue the
use of the protein itself for cargo delivery into cells, we developed an expression system for the C-terminal half of VP22, residues 159-301
(VP22.C1), and purified the protein in high yields. Addition of short
oligonucleotides (ODNs) induced the assembly of novel particles, which
were regular spheres with a size range of 0.3 to 1.0 µm in diameter,
incorporating both protein and ODN. Following the particles in living
cells using fluorescently tagged ODNs, we show that they enter
efficiently within 2-4 h, and reside stably in the cell cytoplasm for
up to several days. Remarkably, however, light activation induced
particle disruption and release of the protein and ODN to the nucleus
and cytoplasm within seconds, a process that we have captured by time
lapse microscopy. In addition to delivering antisense ODNs, ribozymes,
and RNA/DNA hybrids, the VP22.C1 protein could also be modified to
include peptides or proteins. These particles have the potential for
delivery of a wide range of therapeutic agents in gene therapy and
vaccine development.
Particle Formation by a Conserved Domain of the Herpes
Simplex Virus Protein VP22 Facilitating Protein and Nucleic Acid
Delivery*,
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains a supplementary movie.
To whom correspondence should be addressed. Tel.: 44-1883-715028;
Fax: 44-1883-714375; E-mail: P.OHare@mcri.ac.uk.
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