Conserved cytoplasmic domain sequences mediate the ER export of VZV, HSV-1, and HCMV gB

Abstract

Glycoprotein B (gB) is conserved among the herpesviruses and participates in both virus entry and cell-cell spread. The ER export of VZV gB is mediated by two cytoplasmic domain regions, aa 818-826, which contains a YXXphi motif, and the C-terminal 17 aa. The current study examines whether related sequences in the cytoplasmic domains of HSV-1 and HCMV gB similarly influence the ER export of their gB homologs. Directed mutations were introduced into the cytoplasmic domains of HSV-1 and HCMV gB, and the efficiencies with which the mutated proteins acquired Golgi-dependent modifications were determined. Sequences homologous to VZV gB aa 818-826 were required for normal ER export of both HSV-1 gB and HCMV gB. However, the C-terminal regions of HSV-1 and HCMV gB had no impact on ER export. Therefore, alpha- and betaherpesvirus gB homologs share conserved ER export signals, but species-specific differences in the ER export of gB also exist.