More details emerge on the interaction between HHV-6B and its newly discovered cellular receptor, CD134
After discovering a novel human receptor (CD134) used by HHV-6B for cellular entry last year, Dr. Yasuko Mori’s group at Kobe University Graduate School of Medicine in Japan has released additional details regarding the interaction of HHV-6B its newly described receptor.
In an article published in the Journal of Virology earlier this month, the group shows that a cysteine-rich domain (CRD2) of CD134 is critical for binding to the HHV-6B glycoprotein complex, and is required for HHV-6B infection. Furthermore, the group shows that the expression of HHV-6B gQ1 and gQ2 subunits is sufficient for CD134 binding, which is different from the binding of HHV-6A to its receptor, CD46. The group has also outlined the use of a particular region in the HHV-6B gQ1 subunit that is critical for its proper function.
Originally it was believed that CD46 was the receptor for both HHV-6A and HHV-6B. However, recent evidence suggests that distinct mechanisms of cellular entry are at play between the two viruses. Earlier this year, a group from France was able to develop a mouse model of HHV-6A CNS infection by infecting CD46 transgenic mice with HHV-6A. However, the transgenic mice were unable to be infected with HHV-6B.
Professor Yasuko Mori is renowned for her work as a clinical molecular virologist, with particular expertise in the field of HHV-6. She is head of the division of Clinical Virology at Kobe University Graduate School of Medicine, and is a longtime HHV-6 Foundation Scientific Advisory Board member.
For more information, read the full paper.