Resistance is futile: assimilation of cellular machinery by HIV-1.
HIV-1 budding appears to require Vps4 and Tsg101-two proteins that have links to endosomal sorting machinery. A picture emerges wherein divergent viruses recruit endosomal proteins like Tsg101 to gain access to ubiquitin processes that play a crucial role during viral budding.
Perez
O D
OD
Department of Microbiology and Immunology, Stanford School of Medicine, Stanford, CA 94305, USA.
Nolan
G P
GP
D000163:Acquired Immunodeficiency Syndrome / Q000821:virology*; D000251:Adenosine Triphosphatases; D002352:Carrier Proteins / Q000502:physiology*; D004268:DNA-Binding Proteins / Q000502:physiology; D056827:Endosomal Sorting Complexes Required for Transport; D011992:Endosomes / Q000502:physiology; D005656:Fungal Proteins / Q000502:physiology; D015497:HIV-1 / Q000502:physiology*; D006801:Humans; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors / Q000502:physiology; D014779:Virus Replication; D000099177:Tsg101 Protein
D000251:Adenosine Triphosphatases; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D056827:Endosomal Sorting Complexes Required for Transport; D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D000099177:Tsg101 Protein; C107528:VPS4 protein, S cerevisiae