Abstract
Glycoprotein B (gB) is conserved among the herpesvirus family which infects a broad range of species. To investigate the functional homology of human α-herpesviruses, β-herpesviruses, and γ-herpesviruses gB proteins, complementation studies were performed with gB genes from each subfamily member using EBV gp110 (EBV gB homologue) and HSV-1 gB null mutants. Neither the α-herpesvirus HSV-1 gB gene nor the β-herpesvirus HCMV gB gene were able to complement the gp110 null mutant. Conversely, neither the β-herpesvirus HCMV gB or the γ-herpesvirus EBV gp110 gene were able to complement HSV-1 gB null mutants. To further investigate functional domains of EBV gp110 and HSV-1 gB, gB-gp110 chimeric proteins were constructed. Surprisingly, none of the chimeric proteins were able to complement either HSV-1 gB null mutants or EBV gp110 null mutants. These results demonstrate that there is not sufficient functional homology between the different gas to allow complementation in other subfamily members of the herpesvirus family.
| Original language | English |
|---|---|
| Pages (from-to) | 170-181 |
| Number of pages | 12 |
| Journal | Virology |
| Volume | 237 |
| Issue number | 1 |
| DOIs | |
| State | Published - 13 Oct 1997 |
Bibliographical note
Funding Information:R.L. is supported by Public Health Service Grants CA62234 and CA73507 from the National Cancer Institute and a grant from The Council for Tobacco Research Council, U.S.A. R.L. is a Scholar of the Leukemia Society of America. T.C. is supported by PHS Grant AI34998 from the National Institute of Alergy, Immunology and Infectious Disease and by a Basic Research Grant from the March of Dimes Birth Defects Foundation. We gratefully acknowledge Nanette Susmarski in Pat Spear’s laboratory for her help in performing these studies. We are also grateful to Pat Spear, Stanley Person, Thomas Mettenleiter, and William Britt for providing reagents for these studies.