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- Title
Interaction of L-SIGN with Hepatitis C Virus Envelope Protein E2 Up-Regulates Raf-MEK-ERK Pathway.
- Authors
Zhao, Lan-Juan; Wang, Wen; Ren, Hao; Qi, Zhong-Tian
- Abstract
Liver/lymph node-specific intercellular adhesion molecule-3-grabbing integrin (L-SIGN) facilitates hepatitis C virus (HCV) infection through interaction with HCV envelope protein E2. Signaling events triggered by the E2 via L-SIGN are poorly understood. Here, kinase cascades of Raf-MEK-ERK pathway were defined upon the E2 treatment in NIH3T3 cells with stable expression of L-SIGN. The E2 bound to the cells through interaction with L-SIGN and such binding subsequently resulted in phosphorylation and activation of Raf, MEK, and ERK. Blockage of L-SIGN with antibody against L-SIGN reduced the E2-induced phosphorylation of Raf, MEK, and ERK. In the cells infected with cell culture-derived HCV, phosphorylation of these kinases was enhanced by the E2. Up-regulation of Raf-MEK-ERK pathway by HCV E2 via L-SIGN provides new insights into signaling cascade of L-SIGN, and might be a potential target for control and prevention of HCV infection.
- Subjects
HEPATITIS C virus; PROTEINS; ADHESION; KINASES; PHOSPHORYLATION
- Publication
Cell Biochemistry & Biophysics, 2013, Vol 66, Issue 3, p589
- ISSN
1085-9195
- Publication type
Article
- DOI
10.1007/s12013-012-9505-4