title: Proteomics analysis of gastric epithelial AGS cells infected with Epstein-Barr virus.
abstract: Effects of the Epstein-Barr virus (EBV) on cellular protein expression are essential for viral pathogenesis. To characterize the cellular response to EBV infection, differential proteomes of gastric epithelial AGS cells were analyzed with two-dimensional gel electrophoresis (2-DE) followed by matrix-assisted laser desorption/ionization- time of flight (MALDI-TOF) and liquid chromatography electrospray/ionization ion trap (LC-ESI-IT) mass spectrometry identification. Mass spectrometry identified 9 altered cellular proteins, including 5 up-regulated and 4 down-regulated proteins after EBV infection. Notably 2-DE analysis revealed that EBV infection induced increased expression of heat shock cognate 71 kDa protein, actin cytoplasmic 1, pyridoxine-5'-phosphate oxidase, caspase 9, and t-complex protein 1 subunit alpha. In addition, EBV infection considerably suppressed those cellular proteins of zinc finger protein 2, cyclin-dependent kinase 2, macrophage-capping protein, and growth/ differentiation factor 11. Furthermore, the differential expressional levels of partial proteins (cyclin-dependent kinase 2 and caspase 9) were confirmed by Western blot analysis.Thus, this work effectively provided useful protein-related information to facilitate further investigation of the mechanisms underlying EBV infection and pathogenesis.
authors.affiliation: Department of General Surgery, Third Xiangya Hospital, Central South University, Changsha, Hunan Province, China.
authors.forename: Yong
authors.initials: Y
authors.lastname: Ding
authors.forename: Xiao-Rong
authors.initials: XR
authors.lastname: Li
authors.forename: Kai-Yan
authors.initials: KY
authors.lastname: Yang
authors.forename: Li-Hua
authors.initials: LH
authors.lastname: Huang
authors.forename: Gui
authors.initials: G
authors.lastname: Hu
authors.forename: Kai
authors.initials: K
authors.lastname: Gao
mesh_terms: D000199:Actins / Q000378:metabolism; D019485:Bone Morphogenetic Proteins / Q000378:metabolism; D053453:Caspase 9 / Q000378:metabolism; D045744:Cell Line, Tumor; D056404:Chaperonin Containing TCP-1 / Q000378:metabolism; D051357:Cyclin-Dependent Kinase 2 / Q000378:metabolism; D015536:Down-Regulation; D015180:Electrophoresis, Gel, Two-Dimensional; D020031:Epstein-Barr Virus Infections / Q000378:metabolism*; D055412:Growth Differentiation Factors / Q000378:metabolism; D050883:HSC70 Heat-Shock Proteins / Q000378:metabolism; D004854:Herpesvirus 4, Human; D006801:Humans; D051741:Kruppel-Like Transcription Factors / Q000378:metabolism; D008840:Microfilament Proteins / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism; D020543:Proteome / Q000378:metabolism*; D011734:Pyridoxaminephosphate Oxidase / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013274:Stomach Neoplasms / Q000378:metabolism* / Q000821:virology; D015854:Up-Regulation
chemical_list: D000199:Actins; D019485:Bone Morphogenetic Proteins; C492266:GDF11 protein, human; D055412:Growth Differentiation Factors; D050883:HSC70 Heat-Shock Proteins; C494371:HSPA8 protein, human; D051741:Kruppel-Like Transcription Factors; D008840:Microfilament Proteins; D009687:Nuclear Proteins; D020543:Proteome; C533304:TCP1 protein, human; C118913:ZNF2 protein, human; C066575:CAPG protein, human; D011734:Pyridoxaminephosphate Oxidase; D051357:Cyclin-Dependent Kinase 2; D053453:Caspase 9; D056404:Chaperonin Containing TCP-1