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Published on: August 31, 2017
Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic
Andrew R Tait1, Suzana K Straus
1Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC, Canada V6T 1Z1.
Abstract:
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.
Insights
Human Herpesvirus Type 6 protein U24 can be phosphorylated at a site mimicking myelin basic protein
Area of Science:
- Neuroimmunology
- Virology
- Molecular Biology
Background:
- Myelin basic protein (MBP) phosphorylation at Thr97 is reduced in multiple sclerosis (MS).
- This phosphorylation site is crucial for MBP function.
- Human Herpesvirus Type 6 (HHV-6) protein U24 shares a similar sequence to the MBP phosphorylation site.
Purpose of the Study:
- To investigate if HHV-6 U24 protein can be phosphorylated at the threonine residue equivalent to MBP's Thr97.
- To explore the potential role of phospho-U24 in MS pathology.
Main Methods:
- Mass spectrometry
- Thin layer chromatography
- Autoradiography
Main Results:
- Demonstrated that U24 protein can be phosphorylated at the threonine residue analogous to MBP's Thr97.
- Identified phosphorylated U24 (phospho-U24).
Conclusions:
- Phosphorylated U24 may interfere with cellular signaling pathways involving phosphorylated MBP.
- This interference could contribute to the pathological processes observed in multiple sclerosis.
