MAPPING PHOSPHORYLATION SITES IN THE NON-STRUCTURAL PROTEIN 5A FROM HEPATITUS C

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The hepatitis C virus encodes a poorly defined protein termed NS5a. NS5a has been reported to be phosphorylated, but the amino acids modified are not known. Dr. Evans from the Rice laboratory has provided us with an affinity purified version of NS5a from HCV replicon-infected hepatocytes. We used hypothesis-driven mass spectrometry to search for and identify sites of phosphorylation on NS5a. To date, we have identified one novel site of phosphorylation on NS5a. Current efforts on this project: 1) mutate the site of phosphorylation and determine effects on the virus 2) modify the purification techniques for NS5a to allow for purification and mass spectrometric identification of interacting proteins.