Zhou, G. and Roizman, B. (2007) Separation of Receptor-Binding and Profusogenic Domains of Glycoprotein D of Herpes Simplex Virus 1 into Distinct Interacting Proteins. Proceedings of the National Academy of Sciences of the United States of America, 104, 4142-4146.
https://doi.org/10.1073/pnas.0611565104

has been cited by the following article:

• TITLE: Novel Functional Motifs of the Cell Entry Glycoprotein D for Oncolytic Herpes Simplex Viruses

  AUTHORS: Boxu Ren, Xiaoqin Liu, Yingying Wang, Yanning Lyu, Hongyi Xin, Xiaochun Peng, Ying Xiang, Xianwang Wang, Hongwu Xin

  KEYWORDS: Oncolytic Herpes Simplex Virus (oHSV), Amino Acids (AA), Glycoprotein D (gD), Cancer Treatment, Reengineering Virus

  JOURNAL NAME: Yangtze Medicine, Vol.5 No.4, December 28, 2021

  ABSTRACT: Background: Oncolytic herpes simplex virus (oHSV) have been proved effective and safe to treat tumors. Glycoprotein D (gD) has been engineered for targeting cancer cells and de-targeting normal cells successfully, however, the effectiveness and safety of oHSVs still need to be improved. Method: Here we sequenced the DNA encoding gD of our recently isolated new strain HSV-1-LXMW and compared the gD amino acid sequence with the gDs of other 7 HSV-1 and 3 HSV-2 strains. Results: Phylogenetic analysis revealed that HSV-1-LXMW is evolutionarily close to HSV-1-Patton and -KOS strains. The gD amino acid sequence alignment identified 19 conserved and 8 variable regions. We further predicted 10 new motifs in HSV gD for the first time and identified motif differences in HSV-1 and HSV-2. We summarized the gD-engineered oHSVs and found that some of the newly identified gD motifs are actually functional. Conclusion: Our results shed light on HSV gD biology and provided new directions for future gD functional studies and engineering in order to make better oHSVs.