Measles virus phosphoprotein inhibits apoptosis and enhances clonogenic and migratory properties in HeLa cells
- 16 Downloads
Measles virus is the causative agent of measles, a major cause of child mortality in developing countries. Two major proteins, coded by the viral genome, are nucleocapsid protein (N) and phosphoprotein (P). The N protein protects the viral genomic RNA and forms ribonucleoprotein complex (RNP) together with P protein. MeV-P protein recruits the large protein (L), i.e. viral RNA-depended RNA polymerase (RdRp), to ensure viral replication in host cell. Apoptogenic properties of N protein of Edmonston vaccine strain have been established in our lab previously. We investigated the role of MeV-P protein of Edmonston vaccine strain as modulator of apoptosis in cervical cancer cell line (HeLa) and found that MeV-P protein is anti-apoptotic and enhances cell proliferation. Measles virus is considered to be innately oncotropic virus. However, the anti-apoptotic property of MeV-P protein raises important concerns while adopting this virus as an anti-cancer therapeutic tool.
KeywordsAnti-apoptosis cell migration clonogenicity, HeLa cells measles virus phosphoprotein Vimentin
measles virus phosphopreotein
measles virus nucleocapsid protein
N-terminal domain of MeV-P
C-terminal domain of MeV-P
reactive oxygen species
urokinase like plasminogen activator
We are thankful to Prof Martin Billeter for providing the plasmids. We thank Mrs Sarika Gupta for expert assistance with the flow cytometry experiments. Our study was supported by grants, which were received from UGC and DST, India. SB is the recipient of a Senior Research Fellowship of UGC.
- Aref S, Bailey K and Fielding A 2016 Measles to the rescue: a review of oncolytic measles virus. Viruses 8 pii:E294Google Scholar
- Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S and Canard B 2003 The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. J. Biol. Chem. 278 18638–18648CrossRefGoogle Scholar