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Proteomic Analysis of Membrane Fraction of Rhabdomyosarcoma Cells in Response to Early Enterovirus 71 Infection

Enterovirus 71 (EV71) infection is one of epidemic disease in children commonly
in Taiwan. The clinical manifestation of EV71 infection may include acute respiratory
disease, hand foot and mouth disease, herpangina, myocarditis, aseptic meningitis,
acute flaccid paralysis, brainstem or cerebellar encephalitis. EV71 infection usually
occurs through the fecal¡Voral route, leading to viremia and invasion of the skin and
mucosa. Infection is initiated by attachment to putative receptor, which induces
conformational changes in the virus that facilitate translocation of the viral RNA into
the cytoplasm. Some cell surface molecules have been primarily identified for
enterovirus which like poliovirus receptor (CD155), coxsackievirus and adenovirus
receptor, Decay accelerating factor (CD55) belong Echoviruses but no EV71 receptor
has yet been found. Rhabdomyosarcoma cells were used as a model for EV71
infection. We use two-dimensional gel electrophoresis to analyse membrane fraction
from rhabdomyosarcoma cells infected with EV71 at 6 h post infection. Twenty-eight
differentially expressed protein spots were identified. Some lipid-associated protein
slightly change after EV71 infection that may indicate EV71 infection will change
membrane structure of rhabdomyosarcoma cells. And some O-linked glycosylation
proteins were also upregulated after EV71 infection. It is interesting to reveal the role
of these proteins in early EV71 infection and cell response.

Identiferoai:union.ndltd.org:NSYSU/oai:NSYSU:etd-0728109-142101
Date28 July 2009
CreatorsKuo, Tzu-Lei
ContributorsKuang-Hung Cheng, Hsueh-Wei Chang, Hurng-Wen Huang
PublisherNSYSU
Source SetsNSYSU Electronic Thesis and Dissertation Archive
LanguageCholon
Detected LanguageEnglish
Typetext
Formatapplication/pdf
Sourcehttp://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0728109-142101
Rightscampus_withheld, Copyright information available at source archive

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