A herpes simplex virus gD-YFP fusion glycoprotein is transported separately from viral capsids in neuronal axons.

Two models describing how alphaherpesviruses exit neurons differ with respect to whether nucleocapsids and envelope glycoproteins travel toward axon termini separately or as assembled enveloped virions. Recently, a pseudorabies virus glycoprotein D (gD)-green fluorescent protein fusion was found to colocalize with viral capsids, supporting anterograde transport of enveloped virions. Previous antibody staining experiments demonstrated that herpes simplex virus (HSV) glycoproteins and capsids are separately transported in axons. Here, we generated an HSV expressing a gD-yellow fluorescent protein (YFP) fusion and found that gD-YFP and capsids were transported separately in neuronal axons. Anti-gD antibodies colocalized with gD-YFP, indicating that gD-YFP behaves like wild-type HSV gD.