This Article Full Text (PDF) Other Versions of this Article: JVI.02809-06v1 81/11/5985    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Huang, C. Articles by Chang, M.-F. Search for Related Content PubMed PubMed Citation Articles by Huang, C. Articles by Chang, M.-F.

 Previous Article  |  Next Article 

J. Virol. doi:10.1128/JVI.02809-06
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Large Hepatitis Delta Antigen Is a Novel Clathrin Adaptor-like Protein

Institute of Biochemistry and Molecular Biology and Institute of Microbiology, National Taiwan University College of Medicine, Institute of Biochemistry and Molecular Biology, National Yang-Ming University School of Life Sciences, Taipei, Taiwan

^* To whom correspondence should be addressed. Email: mfchang{at}ntumc.org.

	Abstract

Clathrin-mediated endocytosis is a common pathway for viral entry, but little is known about the direct association of viral protein with clathrin in the cytoplasm. In this study, a putative clathrin-box known to be conserved in clathrin adaptors was identified at the C terminus of the large hepatitis delta antigen (HDAg-L). Similar to clathrin adaptors, HDAg-L directly interacted with the N terminus of clathrin heavy chain through the clathrin-box. HDAg-L is a nucleocytoplasmic shuttle protein important for the assembly of hepatitis delta virus (HDV). Here, we demonstrated that brefeldin A and wortmannin, inhibitors of clathrin-mediated exocytosis and endosomal trafficking, respectively, specifically blocked HDV assembly, but had no effect on the assembly of the small surface antigen of hepatitis B Virus. In addition, the cytoplasm-localized HDAg-L inhibited the clathrin-mediated endocytosis of transferrin and the degradation of epidermal growth factor receptor. These results indicate that HDAg-L is a new clathrin adaptor-like protein, it may involve in the maturation and pathogenesis of HDV coinfection or superinfection with hepatitis B virus through interacting with clathrin.