Holton R H, Gentry G A
Department of Microbiology, University of Mississippi Medical Center, Jackson 39216-4505, USA.
Intervirology. 1996;39(4):270-4. doi: 10.1159/000150528.
The Epstein-Barr virus (EBV) BXLF1 fragment open reading frame (LORF), though to encode deoxythymidine kinase (dTK) activity, and a shorter frame (SORF), starting at an internal in-frame AUG, were isolated by polymerase chain reaction from a plasmid containing the EcoR1 fragment of EBV strain FF-41. These were transfected into dTK-Escherichia coli, producing multiple SORF- or LORF-containing colonies, which expressed dTK. The 243 NH2-terminal residues of the LORF-encoded polypeptide thus are not essential for dTK activity. SORF, with 1,092 bp, is predicted to encode a 36- to 37-kD polypeptide, in the size range of other herpesviral dTKs.
爱泼斯坦-巴尔病毒（EBV）BXLF1片段开放阅读框（LORF），虽被认为可编码脱氧胸苷激酶（dTK）活性，以及一个起始于框内内部AUG的较短阅读框（SORF），通过聚合酶链反应从含有EBV FF-41株EcoR1片段的质粒中分离得到。将它们转染到dTK缺陷型大肠杆菌中，产生了多个含有SORF或LORF的菌落，这些菌落表达dTK。因此，LORF编码的多肽的243个氨基末端残基对于dTK活性并非必需。SORF长度为1092 bp，预计可编码一种36至37 kD的多肽，处于其他疱疹病毒dTKs的大小范围内。
