April 23, 2010
The Interaction of Sendai Virus Matrix Protein and Host Cell Proteins
LSAMP VI Bridges to the Doctorate Scholar
The Paramyxoviridae family includes viruses such as measles, mumps, and human parainfluenza viruses, all of which infect vertebrates. Many of these cause respiratory infections in humans. Sendai virus is a negative sense ssRNA enveloped virus belonging to the Paramyxoviridae family. Wild-type (wt) Sendai virus causes a localized respiratory tract infection in mice, while a varient, F1-R, causes a systemic infection. The differences in infection are due to amino acid changes in the F and M proteins of F1-R. The Matrix (M) protein is believed to be the organizer of viral exit from the host cell. M also appears to play other roles in the life cycle of the virus. It serves as a negative regulator of Sendai virus transcription and past studies have demonstrated that M protein interacts with cellular tubulin. TubulinÂs interaction serves to positively regulate transcription of the viral genome by causing M proteinÂs (negative regulator of transcription) removal from the RNP complex. It is believed that M proteinÂs basic N terminal region interacts with tubulinÂs C terminal domain. My aim is to characterize the tubulin-binding domain in Sendai virusÂs M protein by generating point mutations in M protein and testing its tubulin binding ability, compared to wild type M protein, using West-Western and SPR analysis. Host glycolytic factors such phosphoglycerate kinase and enolase have also been shown to play a role in the regulation of viral transcription. I plan to determine if there is any direct interaction between M protein and enolase and M protein and phosphoglycerate kinase. By studying host-pathogen protein interaction we hope to gain a better understanding of viral pathogenesis which could lead to development of new therapeutic inventions.