Proteomic analysis of human immunodeficiency virus using liquid chromatography/tandem mass spectrometry effectively distinguishes specific incorporated host proteins.
A major challenge to studying virus-incorporated host proteins is the fact that they are not encoded by the viral genome. We used Liquid Chromatography/Tandem Mass Spectrometry (LC-MS/MS) on whole virions to obtain a snapshot of the HIV-1 proteome. We identified known viral and host-cellular proteins and also identified novel components of HIV-1 and confirm these by traditional biochemical methods. Our comparison of wild-type and mutant viruses demonstrates that LC-MS/MS has the specificity to distinguish the presence/absence of a single host protein in intact virions.
Saphire
Andrew C S
AC
The Center for Protein Sciences and Department of Immunology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, California 92037, USA.
Gallay
Philippe A
PA
Bark
Steven J
SJ
D000595:Amino Acid Sequence; D015703:Antigens, CD / Q000737:chemistry / Q000378:metabolism; D015153:Blotting, Western; D000071178:CD48 Antigen; D002460:Cell Line; D002853:Chromatography, Liquid; D015497:HIV-1 / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D019169:Jurkat Cells; D008969:Molecular Sequence Data; D025941:Protein Interaction Mapping; D040901:Proteomics / Q000379:methods; D021241:Spectrometry, Mass, Electrospray Ionization; D053719:Tandem Mass Spectrometry; D014764:Viral Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D015703:Antigens, CD; D000071178:CD48 Antigen; D014764:Viral Proteins