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Characterization of cytoplasmic motifs important in rhesus rhadinovirus gB processing and trafficking
Sabine M Lang1, Robert E Means
1Department Of Pathology, Yale University School of Medicine, P.O. Box 208023, New Haven, CT 06520, USA.
Abstract:
Rhesus monkey rhadinovirus (RRV) is highly related to Kaposi's sarcoma-associated herpesvirus (KSHV), a human gamma-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 gamma-herpesvirus assembly and egress.
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