| Title | Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis |
| Publication Type | Journal Article |
| Year of Publication | 2008 |
| Authors | Tait, AR, Straus, SK |
| Journal | Febs Letters |
| Volume | 582 |
| Pagination | 2685-2688 |
| Date Published | Aug |
| Type of Article | Article |
| ISBN Number | 0014-5793 |
| Keywords | BINDING, EXPRESSION, HUMAN-HERPESVIRUS-6, IDENTIFICATION, KINASE, MEMBRANE MICRODOMAINS, mimicry, myelin, PHOSPHORYLATION, POSTTRANSLATIONAL MODIFICATIONS, SITE, T-ANTIGEN, U24 |
| 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. |
| URL | <Go to ISI>://000258108400002 |
