The Epstein-Barr virus glycoprotein 110 carboxy-terminal tail domain is essential for lytic virus replication.
To investigate the importance of the Epstein-Barr virus (EBV) glycoprotein 110 (gp110) tail domain in the intracellular localization of gp110 and virus lytic replication, three carboxy-terminal truncation mutants of gp110 were constructed. Deletion of 16 amino acids from the carboxyl-terminal tail resulted in gp110 intracellular localization which was indistinguishable from that of wild-type gp110, whereas deletion of either 41 or 56 amino acids from the carboxyl-terminal tail of gp110 resulted in loss of retention of gp110 in the endoplasmic reticulum and nuclear membrane. None of the gp110 truncation mutants was able to complement EBV(gp110-)+ lymphoblastoid cell lines in transformation assays, indicating the importance of the gp110 tail domain in virus lytic replication. In electron microscopy analysis, no nucleocapsids or enveloped viruses were detected in EBV(gp110-)+ lymphoblastoid cell lines induced for lytic replication.
Lee
S K
SK
Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 60611, USA.
Longnecker
R
R
D000595:Amino Acid Sequence; D004854:Herpesvirus 4, Human / Q000502:physiology*; D008213:Lymphocyte Activation; D008969:Molecular Sequence Data; D009154:Mutation; D014764:Viral Proteins / Q000502:physiology*; D014779:Virus Replication
C060207:Epstein-Barr virus glycoprotein gp110; D014764:Viral Proteins