Abstract
Herpes simplex virus (HSV) helper functions for (AAV) replication comprise HSV ICP8 and helicase-primase UL5/UL52/UL8. Here we show that N-terminal amino acids of AAV Rep78 that contact the Rep-binding site within the AAV inverted terminal repeat (ITR) are required for ternary-complex formation with infected-cell protein 8 (ICP8) on AAV single-strand DNA (ssDNA) in vitro and for colocalization in nuclear replication domains in vivo. Our data suggest that HSV-dependent AAV replication is initiated by Rep contacting the AAV ITR and by cooperative binding of ICP8 on AAV ssDNA.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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DNA Helicases / chemistry
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DNA Helicases / genetics
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DNA Helicases / metabolism*
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DNA Replication
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Dependovirus / chemistry
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Dependovirus / enzymology*
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Dependovirus / genetics
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Dependovirus / physiology
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HeLa Cells
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Helper Viruses / genetics
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Helper Viruses / metabolism
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Humans
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Parvoviridae Infections / virology
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Protein Structure, Tertiary
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Protein Transport
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Simplexvirus / genetics
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Simplexvirus / metabolism*
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Terminal Repeat Sequences*
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Viral Proteins / chemistry
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Viral Proteins / genetics
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Viral Proteins / metabolism*
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Virus Replication
Substances
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DNA-Binding Proteins
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ICP8 protein, Simplexvirus
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Viral Proteins
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DNA Helicases