کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
3424296 | 1227211 | 2012 | 10 صفحه PDF | دانلود رایگان |
Human immunodeficiency virus (HIV-1) depends upon host-encoded proteins to facilitate its replication while at the same time inhibiting critical components of innate and/or intrinsic immune response pathways. To characterize the host cell response on protein levels in CD4+ lymphoblastoid SUP-T1 cells after infection with HIV-1 strain LAI, we used mass spectrometry (MS)-based global quantitation with iTRAQ (isobaric tag for relative and absolute quantification). We found 266, 60 and 22 proteins differentially expressed (DE) (P-value≤0.05) at 4, 8, and 20 hours post-infection (hpi), respectively, compared to time-matched mock-infected samples. The majority of changes in protein abundance occurred at an early stage of infection well before the de novo production of viral proteins. Functional analyses of these DE proteins showed enrichment in several biological pathways including protein synthesis, cell proliferation, and T-cell activation. Importantly, these early changes before the time of robust viral production have not been described before.
► We measured proteome changes in HIV-infected T-cells in a synchronized infection.
► Mass spectrometry-based global iTRAQ was used to quantify these changes.
► 348 proteins involved in various key cellular functions changed at early hours.
► Importantly, these protein level changes occur before the onset of robust viral production.
► Such early changes have not been described before.
Journal: Virology - Volume 429, Issue 1, 20 July 2012, Pages 37–46