Prototype Foamy Virus ( PFV ) Gag nuclear localization – A novel pathway among 1 retroviruses 2 3

نویسندگان

  • Erik Müllers
  • Kristin Stirnnagel
  • Sylvia Kaulfuß
  • Dirk Lindemann
چکیده

1 Prototype Foamy Virus (PFV) Gag nuclear localization – A novel pathway among 1 retroviruses 2 3 Erik Müllers, Kristin Stirnnagel, Sylvia Kaulfuß, and Dirk Lindemann* 4 5 Institut für Virologie, Medizinische Fakultät "Carl Gustav Carus", Technische Universität 6 Dresden, Dresden, CRTD / DFG-Center for Regenerative Therapies Dresden Cluster of 7 Excellence, Biotechnology Center, Dresden, Germany. 8 9 *Corresponding author: 10 Dirk Lindemann 11 Institut für Virologie 12 Medizinische Fakultät "Carl Gustav Carus" 13 Technische Universität Dresden 14 Fetscherstr. 74 15 01307 Dresden, Germany 16 Phone: +49-351-458-6210 17 FAX: +49-351-458-6314 18 E-mail: [email protected] 19 Running title: Foamy virus Gag nuclear localization 20 Abstract word count: 241 Text word count: 5898 21 Copyright © 2011, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved. J. Virol. doi:10.1128/JVI.00663-11 JVI Accepts, published online ahead of print on 29 June 2011

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Nuclear Localization Signals in Prototype Foamy Viral Integrase for Successive Infection and Replication in Dividing Cells

We identified four basic amino acid residues as nuclear localization signals (NLS) in the C-terminal domain of the prototype foamy viral (PFV) integrase (IN) protein that were essential for viral replication. We constructed seven point mutants in the C-terminal domain by changing the lysine and arginine at residues 305, 308, 313, 315, 318, 324, and 329 to threonine or proline, respectively, to ...

متن کامل

Characterization of prototype foamy virus gag late assembly domain motifs and their role in particle egress and infectivity.

Foamy viruses (FV) are unusual among retroviruses since they require both Gag and Env structural proteins for particle egress. Recently significant progress has been made towards the mechanistic understanding of the viral release process, in particular that of retroviruses, and the viral domains and cellular pathways involved. However little is currently known about domains of FV structural pro...

متن کامل

Interactions of Prototype Foamy Virus Capsids with Host Cell Polo-Like Kinases Are Important for Efficient Viral DNA Integration

Unlike for other retroviruses, only a few host cell factors that aid the replication of foamy viruses (FVs) via interaction with viral structural components are known. Using a yeast-two-hybrid (Y2H) screen with prototype FV (PFV) Gag protein as bait we identified human polo-like kinase 2 (hPLK2), a member of cell cycle regulatory kinases, as a new interactor of PFV capsids. Further Y2H studies ...

متن کامل

Human Pirh2 is A Novel Inhibitor of Prototype Foamy Virus Replication

Prototype foamy virus (PFV) is a member of the unconventional and nonpathogenic retroviruses. PFV causes lifelong chronic infections, which are partially attributable to a number of host cell factors that restrict viral replication. Herein, we identified human p53-induced RING-H2 protein (Pirh2) as a novel inhibitor of prototype foamy virus. Overexpression of Pirh2 decreased the replication of ...

متن کامل

Cytoplasmic utilization of human immunodeficiency virus type 1 genomic RNA is not dependent on a nuclear interaction with gag.

In some retroviruses, such as Rous sarcoma virus and prototype foamy virus, Gag proteins are known to shuttle between the nucleus and the cytoplasm and are implicated in nuclear export of the viral genomic unspliced RNA (gRNA) for subsequent encapsidation. A similar function has been proposed for human immunodeficiency virus type 1 (HIV-1) Gag based on the identification of nuclear localization...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2011