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J Gen Virol 85 (2004), 921-927; DOI 10.1099/vir.0.19576-0

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© 2004 Society for General Microbiology

The central region of human immunodeficiency virus type 1 p6 protein (Gag residues S14–I31) is dispensable for the virus in vitro

Gabriela Bleiber1, Solange Peters1, Raquel Martinez1, Dusan Cmarko3, Pascal Meylan1,2 and Amalio Telenti1,2

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 S14–I31 (p6Gag) and R20–D39 (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 ({Delta}R20–D39, 42 % of p6Pol) did not alter protease autocleavage.




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