A Bipartite Late-Budding Domain in Human Immunodeficiency Virus Type 1
AUTOR(ES)
Martin-Serrano, Juan
FONTE
American Society for Microbiology
RESUMO
Human immunodeficiency virus type 1 (HIV-1) encodes a PTAP motif within the p6 domain of Gag that recruits Tsg101 and associated factors to facilitate virion budding. In this study, we use trans-complementation assays to demonstrate that the PTAP motif acts synergistically with additional p6 sequences to mediate the formation of infectious extracellular HIV-1 virions. These studies suggest that Tsg101 recruitment is necessary but not sufficient to account for late-budding activity exhibited by HIV-1 p6.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=254264Documentos Relacionados
- Functional Analysis of Late-Budding Domain Activity Associated with the PSAP Motif within the Vesicular Stomatitis Virus M Protein
- Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
- The Late Domain of Human Immunodeficiency Virus Type 1 p6 Promotes Virus Release in a Cell Type-Dependent Manner
- The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells.
- Human immunodeficiency virus type 2 glycoprotein enhancement of particle budding: role of the cytoplasmic domain.