Exploring the Pathogenic Potential of c-fos, Polyoma Middle T and Human Foamy Virus in Transgenic Mice

Author(s):  
Erwin F. Wagner ◽  
Adriano Aguzzi
Science ◽  
1991 ◽  
Vol 253 (5019) ◽  
pp. 555-557 ◽  
Author(s):  
K Bothe ◽  
A Aguzzi ◽  
H Lassmann ◽  
A Rethwilm ◽  
I Horak

The Lancet ◽  
1994 ◽  
Vol 343 (8898) ◽  
pp. 666 ◽  
Author(s):  
Ali Saib ◽  
Martine Canivet ◽  
Marie-Louise Giron ◽  
Françis Bolgert ◽  
Joceline Valla ◽  
...  

1998 ◽  
Vol 72 (7) ◽  
pp. 5510-5516 ◽  
Author(s):  
Otto Erlwein ◽  
Paul D. Bieniasz ◽  
Myra O. McClure

ABSTRACT A series of vectors with heterologous genes was constructed from HSRV1, an infectious clone of human foamy virus (HFV), and transfected into baby hamster kidney cells to generate stably transfected vector cell lines. Two cis-acting sequences were required to achieve efficient rescue by helper virus. The first element was located at the 5′ end upstream of position 1274 of the proviral DNA. Interestingly, a mutation in the leader sequence which decreased the ability to dimerize in vitro inhibited transfer by helper HFV. A second element that was important for vector transfer was located in thepol gene between positions 5638 and 6317. Constructs lacking this element were only poorly transferred by helper HFV, even though their RNA was produced in the vector cell lines. This finding rules out the possibility that the observed lack of transfer was due to RNA instability. A minimal vector containing only these two elements could be successfully delivered by helper HFV, confirming that all essential cis-acting sequences were present. The presence of a sequence described as a second polypurine tract in HFV was not necessary for transfer. Our data identified the minimal sequence requirements for HFV vector transfer for the development of useful vector systems.


Stem Cells ◽  
1997 ◽  
Vol 15 (S2) ◽  
pp. 141-147 ◽  
Author(s):  
Jochen Bodem ◽  
Martin Löchelt ◽  
Ping Yang ◽  
Rolf M. Flügel

2001 ◽  
Vol 75 (9) ◽  
pp. 4367-4375 ◽  
Author(s):  
Joelle Tobaly-Tapiero ◽  
Patricia Bittoun ◽  
Marie-Lou Giron ◽  
Manuel Neves ◽  
Marcel Koken ◽  
...  

ABSTRACT Retroviral Gag expression is sufficient for capsid assembly, which occurs through interaction between distinct Gag domains. Human foamy virus (HFV) capsids assemble within the cytoplasm, although their budding, which mainly occurs in the endoplasmic reticulum, requires the presence of homologous Env. Yet little is known about the molecular basis of HFV Gag precursor assembly. Using fusions between HFV Gag and a nuclear reporter protein, we have identified a strong interaction domain in the N terminus of HFV Gag which is predicted to contain a conserved coiled-coil motif. Deletion within this region in an HFV provirus abolishes viral production through inhibition of capsid assembly.


Sign in / Sign up

Export Citation Format

Share Document