Abstract
We show that the HSV-1 structural protein VP22 has the remarkable property of intercellular transport, which is so efficient that following expression in a subpopulation the protein spreads to every cell in a monolayer, where it concentrates in the nucleus and binds chromatin. VP22 movement was observed both after delivery of DNA by transfection or microinjection and during virus infection. Moreover, we demonstrate that VP22 trafficking occurs via a nonclassical Golgi-independent mechanism. Sensitivity to cytochalasin D treatment suggests that VP22 utilizes a novel trafficking pathway that involves the actin cytoskeleton. In addition, we demonstrate intercellular transport of a VP22 fusion protein after endogenous synthesis or exogenous application, indicating that VP22 may have potential in the field of protein delivery.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actin Cytoskeleton / metabolism
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Amino Acid Sequence
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Animals
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Biological Transport / drug effects
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COS Cells
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Cell Line
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Cell Nucleus / metabolism*
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Chromatin / metabolism
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Cytochalasin D / pharmacology
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Cytoplasm / metabolism
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Endocytosis
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Endoplasmic Reticulum / metabolism
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Golgi Apparatus / metabolism
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Green Fluorescent Proteins
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Herpesvirus 1, Human / physiology*
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Intermediate Filaments / metabolism
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Luminescent Proteins / metabolism
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Microtubules / metabolism
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Molecular Sequence Data
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Recombinant Fusion Proteins / metabolism*
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Transfection
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Viral Structural Proteins / chemistry
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Viral Structural Proteins / genetics
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Viral Structural Proteins / metabolism*
Substances
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Chromatin
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Luminescent Proteins
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Recombinant Fusion Proteins
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Viral Structural Proteins
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herpes simplex virus type 1 protein VP22
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Green Fluorescent Proteins
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Cytochalasin D