|
|
||||||||
1 Division of Infectious Diseases, University of Lausanne, Lausanne, Switzerland
2 Institute of Microbiology, University of Lausanne, Lausanne, Switzerland
3 University Hospital, and Center of Electron Microscopy, University of Lausanne, Lausanne, Switzerland
Correspondence
Amalio Telenti
amalio.telenti{at}hospvd.ch
The human immunodeficiency virus type 1 p6 region encodes p6Gag and the transframe p6Pol protein. The Gag frame encodes an N-terminal late assembly L domain and a C-terminal Vpr binding domain. In the Pol frame, substitution at a C-terminal motif decreases protease autocleavage. The role of the highly polymorphic central region of p6, comprising amino acids S14I31 (p6Gag) and R20D39 (p6Pol), is unclear. Analysis of this central region demonstrated that 35 % of p6Gag appears to be dispensable for virus propagation in vitro and smaller deletion and insertion polymorphisms can be tolerated in vivo. Extensive Pol deletion (
R20D39, 42 % of p6Pol) did not alter protease autocleavage.
This article has been cited by other articles:
![]() |
H.-C. Chiu, F.-D. Wang, Y.-M. A. Chen, and C.-T. Wang Effects of human immunodeficiency virus type 1 transframe protein p6* mutations on viral protease-mediated Gag processing J. Gen. Virol., July 1, 2006; 87(7): 2041 - 2046. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. E. Ott, L. V. Coren, T. D. Gagliardi, and K. Nagashima Heterologous Late-Domain Sequences Have Various Abilities To Promote Budding of Human Immunodeficiency Virus Type 1 J. Virol., July 15, 2005; 79(14): 9038 - 9045. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |