@article{mbs:/content/journal/jgv/10.1099/vir.0.19576-0, author = "Bleiber, Gabriela and Peters, Solange and Martinez, Raquel and Cmarko, Dusan and Meylan, Pascal and Telenti, Amalio", title = "The central region of human immunodeficiency virus type 1 p6 protein (Gag residues S14–I31) is dispensable for the virus in vitro", journal= "Journal of General Virology", year = "2004", volume = "85", number = "4", pages = "921-927", doi = "https://doi.org/10.1099/vir.0.19576-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.19576-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "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 (ΔR20–D39, 42 % of p6Pol) did not alter protease autocleavage.", }