|Mao, Yaopan - MICHIGAN STATE UNIVERSITY|
|Wu, Ping - MICHIGAN STATE UNIVERSITY|
Submitted to: International Marek's Disease Symposium Abstracts and Proceedings
Publication Type: Proceedings
Publication Acceptance Date: September 7, 1996
Publication Date: N/A
Technical Abstract: DNA sequences of Marek's disease virus (MDV) EcoRI fragment E, BamHI fragment P2, J and I1 have been determined and they constitute one large open reading frame (ORF). Analysis of the ORF reveals that it is homologous to the UL36 genes of herpes simplex virus type-1 (HSV), which encodes ICP1/2, a DNA-binding tegument protein. Compared with HSV ICP1/2, the predicted amino acid sequence of the MDV UL36 homolog (UL36h) also contains two potential ATP-binding motifs and a long stretch of proline repeat near its C-terminus, and the two leucine zippers found in HSV UL36 protein are not identified in the UL36h protein. Interestingly, a potential lipid membrane attachment motif is identified at the N terminus of the protein. Based on the known function of the HSV UL36 gene, MDV UL36h may also be involved in DNA packaging during viral maturation.