Quantitative Proteomic Analysis of A549 Cells Infected with Human Respiratory Syncytial Virus

Munday, Diane C.; Emmott, Edward; Surtees, Rebecca; Lardeau, Charles-Hugues; Wu, Weining; Duprex, W. Paul; Dove, Brian K.; Barr, John N.; Hiscox, Julian A.

Respiratory Complex 1 proteins and other mitochondrial proteins identified and quantified by LC-MS/MS (Fig. 6) were decreased in abundance by 2-fold or more in HRSV-infected cells in comparison with mock-infected cells. For example, respiratory Complex 1 protein NDUFB10 was 60-fold decreased in the nuclear fraction but not represented in the cytoplasmic fraction. The abundance of the translocase of the outer mitochondrial membrane (TOM) complex subunits Tom20, Tom22, Tom40, and Tom70 were decreased ϳ129-, 26-, 15-, and 12-fold, respectively, in the nuclear fraction enriched from HRSV-infected cells but were not detected in Table 8. the cytoplasmic fraction. The abundance of voltage-dependent anion channel (VDAC) proteins 1, 2, and 3 were decreased by ϳ31-, 42-, and 26-fold, respectively, in the nuclear fraction in HRSV-infected cells compared with mock-infected cells. VDAC1 and VDAC2 were also detected in the cytoplasmic fraction with 10-and 9-fold increases, respectively, in HRSV-infected cells when compared with mock-infected cells. Prohibitin (PHB) subunits PHB1 and PHB2, which are involved in cell proliferation and the functional integrity of mitochondria (48, 49) , were increased 3-fold in the cytoplasmic fraction from HRSV-infected cells.