Current Approaches on Viral Infection: Proteomics and Functional Validations

Zheng, Jie; Tan, Boon Huan; Sugrue, Richard; Tang, Kai

Besides Heat shock protein 27, other heat shock proteins are also known to be closely involved in the dynamics of virus and host interactions. Heat shock proteins 40 and 70 were identified by proteomics as binding partners of hepatitis C viral protein NS5A. Gonzalez et al. (2009) used quercetin to inhibit the activities of host factor HSPs upon HCV infection. Both viral replication and release were found to be greatly reduced in a dose-dependent manner compared to a mock group. In another study, heat shock protein 90 (hsp90) was identified to be associated with RSV particles by LC-MS/MS (Radhakrishnan et al., 2010) . Immunofluorescence imaging revealed the co-localization of hsp90 with viral filaments and two drug inhibitors, geldanamycin and 17allylaminogeldanamycin, were used to examine hsp90's role during virus infection. Viral filamentous staining patterns were greatly impaired while treated with these two inhibitors. Also, the efficiency of virus infectivity and transmission, indicated by estimating numbers of virus infected cells, were reduced by fivefold when treated with these drugs. Although most cellular heat shock proteins function at transcription or replication levels, the lowabundant hsp90 present inside the RSV plays a major role in the formation of virus filaments and virus transmission.