Characterization of cytoplasmic motifs important in rhesus rhadinovirus gB processing and trafficking

Abstract Rhesus monkey rhadinovirus (RRV) is highly related to Kaposi's sarcoma-associated herpesvirus (KSHV), a human γ-herpesvirus etiologically-linked with several cancers. Glycoprotein B (gB) homologues are encoded by all herpesviruses and play a role in virus attachment, entry, and in egress. We have found that RRV gB, like KSHV gB, is cleaved at a consensus furin cleavage site and is modified by both N-linked and O-linked glycosylation. Mutagenesis of three tyrosine- based trafficking motifs, a diacidic tyrosine motif, and a di-lucine motif in the cytoplasmic region revealed a role for these sequences in both ER export and endocytosis from the plasma membrane. These experiments provide a basis for further experiments looking at gB incorporation and role in γ-herpesvirus assembly and egress.