Proteomics study of N-acetylcysteine response in H1N1-infected cells by using mass spectrometry.
Rapid Commun Mass Spectrom. 2014 Apr 15 ;28(7):741-9. PMID: 24573805
RATIONALE: The pathology of A/Puerto Rico/8/1934 (H1N1) infection associated with the interaction of virus and its host cells is not clear. N-Acetylcysteine (NAC) is an antioxidant as well as a premier antitoxin and immune support substance. A high dose of NAC was recently reported for a therapy of H1N1 (2009) influenza pneumonia.
METHODS: NAC was used as a small-molecule organic probe to investigate the protein expression of human lung carcinoma cell line (A549) infected by influenza virus A/Puerto Rico/8/1934 (H1N1). Differential proteins were identified from MALDI-TOF MS and Q-TOF MS/MS analyses.
RESULTS: The obtained results showed that NAC kept cells away from apoptosis. Virus-infected cells were arrested in G0/G1 phase. The lowest cell population of G0/G1 phase was detected when the cells were treated by 10 mM NAC for one day. Application of MS-based proteomics allowed the identification of the differential proteins. Software analysis showed that four proteins had close relationship.
CONCLUSIONS: The results indicated that NAC as a small-molecule probe might effect the protein expression of A549 cells infected by the H1N1 virus.