Proteomic analysis of human immunodeficiency virus using liquid chromatography/tandem mass spectrometry effectively distinguishes specific incorporated host proteins
| Autor: | Philippe Gallay, Steven J. Bark, Andrew C. S. Saphire |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Proteomics
Spectrometry Mass Electrospray Ionization viruses Mutant Blotting Western Molecular Sequence Data Biology CD48 Antigen Tandem mass spectrometry Biochemistry Genome Cell Line Jurkat Cells Viral Proteins Liquid chromatography–mass spectrometry Antigens CD Tandem Mass Spectrometry Protein Interaction Mapping Humans Amino Acid Sequence Host protein General Chemistry Molecular biology Proteome HIV-1 Bottom-up proteomics Chromatography Liquid |
| Zdroj: | Journal of proteome research. 5(3) |
| ISSN: | 1535-3893 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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