Publication: Proteomic analysis of host responses in HepG2 cells during dengue virus infection
Issued Date
2007-12-01
Resource Type
ISSN
15353893
Other identifier(s)
2-s2.0-38049044738
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Journal of Proteome Research. Vol.6, No.12 (2007), 4592-4600
Suggested Citation
Sa Nga Pattanakitsakul, Kamonthip Rungrojcharoenkit, Rattiyaporn Kanlaya, Supachok Sinchaikul, Sansanee Noisakran, Shui Tein Chen, Prida Malasit, Visith Thongboonkerd Proteomic analysis of host responses in HepG2 cells during dengue virus infection. Journal of Proteome Research. Vol.6, No.12 (2007), 4592-4600. doi:10.1021/pr070366b Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/24073
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Proteomic analysis of host responses in HepG2 cells during dengue virus infection
Abstract
Dengue virus infection remains a public health problem worldwide. However, its pathogenic mechanisms and pathophysiology are still poorly understood. We performed proteomic analysis to evaluate early host responses (as indicated by altered proteins) in human target cells during dengue virus infection. HepG2 cells were infected with dengue virus serotype 2 (DEN-2) at multiplicity of infection (MOI) of 0.1, 0.5, and 1.0. Quantitative analyses of DEN-2 infection and cell death at 12, 24, and 48 h postinfection showed that the MOI of 1.0 with 24 h postinfection duration was the optimal condition to evaluate early host responses, as this condition provided the high %Infection (∼80%), while %Cell death (∼20%) was comparable to that of the mock-control cells. Proteins derived from the mock-control and DEN-2-infected cells were resolved by 2-D PAGE (n = 5 gels for each group) and visualized by SYPRO Ruby stain. Quantitative intensity analysis revealed 17 differentially expressed proteins, which were successfully identified by peptide mass fingerprinting. Most of these altered proteins were the key factors involved in transcription and translation processes. Further functional study on these altered proteins may lead to better understanding of the pathogenic mechanisms and host responses to dengue virus infection, and also to the identification of new therapeutic targets for dengue virus infection. © 2007 American Chemical Society.