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Nucleic Acids Research, 2003, Vol. 31, No. 21 6206-6213
© 2003 Oxford University Press

ssDNA-dependent colocalization of adeno-associated virus Rep and herpes simplex virus ICP8 in nuclear replication domains

Regine Heilbronn*, Markus Engstler1, Stefan Weger, Antje Krahn, Christian Schetter and Michael Boshart*,1

Institut für Infektionsmedizin, Abt. Virologie, Charité Campus Benjamin Franklin, Freie Universität Berlin, Germany and 1 Department Biologie I, Genetik, Ludwig-Maximilians-Universität München, Germany

*To whom correspondence should be addressed. Tel: +49 30 8445 3696; Fax: +49 30 8445 4485; Email: heilbronn{at}ukbf.fu-berlin.de or Tel: +49 89 2180 6155; Fax: +49 89 2180 63853; Email: boshart{at}lmu.de

The subnuclear distribution of replication complex proteins is being recognized as an important factor for the control of DNA replication. Herpes simplex virus (HSV) single-strand (ss)DNA-binding protein, ICP8 (infected cell protein 8) accumulates in nuclear replication domains. ICP8 also serves as helper function for the replication of adeno-associated virus (AAV). Using quantitative 3D colocalization analysis we show that upon coinfection of AAV and HSV the AAV replication protein Rep and ICP8 co-reside in HSV replication domains. In contrast, Rep expressed by a recombinant HSV, in the absence of AAV DNA, displayed a nuclear distribution pattern distinct from that of ICP8. Colocal ization of Rep and ICP8 was restored by the reintroduction of single-stranded AAV vector genomes. In vitro, ICP8 displayed direct binding to Rep78. Single-stranded recombinant AAV DNA strongly stimulated this interaction, whereas double-stranded DNA was ineffective. Our findings suggest that ICP8 by its strong ssDNA-binding activity exploits the unique single-strandedness of the AAV genome to form a tripartite complex with Rep78 and AAV ssDNA. This novel mechanism for recruiting components of a functional replication complex directs AAV to subnuclear HSV replication compartments where the HSV replication complex can replicate the AAV genome.


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