Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis.
Myelin basic protein (MBP) from multiple sclerosis (MS) patients contains lower levels of phosphorylation at Thr97 than normal individuals. The significance of phosphorylation at this site is not fully understood, but it is proposed to play a role in the normal functioning of MBP. Human Herpesvirus Type 6 encodes the protein U24, which has tentatively been implicated in the pathology of MS. U24 shares a 7 amino acid stretch encompassing the Thr97 phosphorylation site of MBP: PRTPPPS. We demonstrate using a combination of mass spectrometry, thin layer chromatography and autoradiography, that U24 can be phosphorylated at the equivalent threonine. Phospho-U24 may confound signalling or other pathways in which phosphorylated MBP may participate, precipitating a pathological process.
Tait
Andrew R
AR
Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC, Canada V6T 1Z1.
Straus
Suzana K
SK
D001483:Base Sequence; D002855:Chromatography, Thin Layer; D015654:Herpesvirus 6, Human / Q000378:metabolism*; D006801:Humans; D020929:Mitogen-Activated Protein Kinase Kinases; D018716:Molecular Mimicry; D009103:Multiple Sclerosis / Q000378:metabolism* / Q000821:virology*; D004676:Myelin Basic Protein / Q000378:metabolism*; D019606:Phosphoamino Acids / Q000032:analysis; D010766:Phosphorylation; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013912:Threonine / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*
D004676:Myelin Basic Protein; D019606:Phosphoamino Acids; D014764:Viral Proteins; D013912:Threonine; D020929:Mitogen-Activated Protein Kinase Kinases