Journal
VIROLOGY
Volume 429, Issue 1, Pages 37-46Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2012.03.026
Keywords
Protein quantification; iTRAQ; HIV-1; T-cells; LC-MS/MS; Ribosomal proteins
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Funding
- Public Health Service from the National Institutes of Health [P30DA015625, P51RR000166, R24 RR016354]
- University of Washington's Proteomics Resource [UWPR95794]
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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. Published by Elsevier Inc.
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