Influenza A virus is well known for its severe clinical consequences. Structurally, this virus is made up of a lipid bilayer embedded with HA, NA and M2 proteins and a core containing eight viral ribonucleoprotein (RNP) complexes. In a typical RNP complex, the nucleoprotein binds with RNA in a non specific manner. The nucleoprotein plays a vital role in transcription, replication, and packaging of RNA during infection. This study aims that NP of A/PR/8/34(H1N1) virus and A/NY/55/2004(H3N2) virus interact with different host proteins depending on cell lines and virus strains. Monoclonal antibodies targeting the nucleoprotein of these viruses have been used for immunoprecipitation and the interacting proteins were identified by mass spectrometry. Tow proteins from the cytoplasm (elongation factor 1 sigma, and Mov10 protein) and 3 proteins from the nucleus (heat shock protein70, hnRNP K protein, and anti alpha actinin 4) were found in all the viral infected cells, and were chosen for validation study. This study will help to understand the virus-host interactions in a better way and may open the gateway for the synthesis of new antiviral drugs which can block these interactions, hence controlling the infection.
| Identifer | oai:union.ndltd.org:MANITOBA/oai:mspace.lib.umanitoba.ca:1993/21939 |
| Date | 24 July 2013 |
| Creators | Almutairi, Saeedah |
| Contributors | Kevin, Coombs (Medical Microbiology), keith, Fowke (Medical Microbiology) John, Wilkins (Biochemistry & Medical Genetics) |
| Source Sets | University of Manitoba Canada |
| Detected Language | English |
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