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Journal of Virology, April 2008, p. 3803-3808, Vol. 82, No. 7
0022-538X/08/$08.00+0     doi:10.1128/JVI.02532-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

E4Orf6-E1B-55k-Dependent Degradation of De Novo-Generated Adeno-Associated Virus Type 5 Rep52 and Capsid Proteins Employs a Cullin 5-Containing E3 Ligase Complex{triangledown}

Ramnath Nayak, K. David Farris, and David J. Pintel*

Department of Molecular Microbiology and Immunology, University of Missouri—Columbia, School of Medicine, Life Sciences Center, Columbia, Missouri 65211

Received 27 November 2007/ Accepted 17 January 2008

Degradation of de novo-generated adeno-associated virus type 5 (AAV5) Rep52 and capsid proteins is part of the limited target specificity displayed by adenovirus type 5 E4Orf6-E1B-55k as part of a cullin 5-containing E3 ligase complex. Both Rep and capsid proteins can be found in the ligase complex, and their presence is dependent on interaction between E4Orf6 and elongins B and C. Degradation of AAV5 proteins can be inhibited by a dominant-negative ubiquitin that prevents chain elongation or by small interfering RNA directed against cullin 5.


* Corresponding author. Mailing address: 471f Life Sciences Center, University of Missouri—Columbia, 1201 Rollins Rd., Columbia, MO 65211. Phone: (573) 882-3920. Fax: (573) 884-9676. E-mail: pinteld{at}missouri.edu

{triangledown} Published ahead of print on 23 January 2008.


Journal of Virology, April 2008, p. 3803-3808, Vol. 82, No. 7
0022-538X/08/$08.00+0     doi:10.1128/JVI.02532-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.







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