|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|
|Type of Article||Article|
|Keywords||BINDING, EXPRESSION, HUMAN-HERPESVIRUS-6, IDENTIFICATION, KINASE, MEMBRANE MICRODOMAINS, mimicry, myelin, PHOSPHORYLATION, POSTTRANSLATIONAL MODIFICATIONS, SITE, T-ANTIGEN, U24|
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|