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Varicella Zoster Virus ORF25 Gene Product: An Essential Hub Protein Linking Encapsidation Proteins and the Nuclear Egress Complex

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Maria G. Vizoso Pinto*†, Venkata R. Pothineni†, Rudolf Haase†, Mathias Woidy‡, Amelie S. Lotz-Havla‡, Søren W. Gersting‡, Ania C. Muntau‡, Jürgen Haas†§, Marvin Sommer

, Ann M. Arvin

, and Armin Baiker†

Max von Pettenkofer-Institute, Ludwig-Maximilians-University, Munich, Germany

Department of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig-Maximilians-University, Munich, Germany

Division of Pathway Medicine, University of Edinburgh, United Kingdom

Department of Pediatrics, Stanford University, Stanford, California, United States

Bavarian Health and Food Safety Authority, Oberschleissheim, Germany

J. Proteome Res., 2011, 10 (12), pp 5374–5382

DOI: 10.1021/pr200628s

Publication Date (Web): October 10, 2011

Max von Pettenkofer-Institute, Department of Virology, Pettenkoferstr. 9a, 80336, Munich, Germany. Phone: +49-(0)89-5160-5231. Fax: +49-(0)89-5160-5292. E-mail: vizoso@mvp.uni-muenchen.de. guadalupevizoso@yahoo.com.

Section:

Microbial, Algal, and Fungal Biochemistry

Abstract

Varicella zoster virus (VZV) ORF25 is a 156 amino acid protein belonging to the approximately 40 core proteins that are conserved throughout the Herpesviridae. By analogy to its functional orthologue UL33 in Herpes simplex virus 1 (HSV-1), ORF25 is thought to be a component of the terminase complex. To investigate how cleavage and encapsidation of viral DNA links to the nuclear egress of mature capsids in VZV, we tested 10 VZV proteins that are predicted to be involved in either of the two processes for protein interactions against each other using three independent protein–protein interaction (PPI) detection systems: the yeast-two-hybrid (Y2H) system, a luminescence based MBP pull-down interaction screening assay (LuMPIS), and a bioluminescence resonance energy transfer (BRET) assay. A set of 20 interactions was consistently detected by at least 2 methods and resulted in a dense interaction network between proteins associated in encapsidation and nuclear egress. The results indicate that the terminase complex in VZV consists of ORF25, ORF30, and ORF45/42 and support a model in which both processes are closely linked to each other. Consistent with its role as a central hub for protein interactions, ORF25 is shown to be essential for VZV replication.