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J Virol, June 1998, p. 4571-4579, Vol. 72, No. 6
Department of Molecular Biology, Princeton
University, Princeton, New Jersey 08544
Received 1 December 1997/Accepted 11 February 1998
Several groups have reported that certain herpesvirus envelope
proteins do not remain on the surface of cells that express them but
rather are internalized by endocytosis in a recycling process. The
biological function of membrane protein endocytosis in the virus life
cycle remains a matter of speculation and debate. In this report, we
demonstrate that some, but not all, membrane proteins encoded by the
alphaherpesvirus pseudorabies virus (PRV) are internalized after
reaching the plasma membrane. Glycoproteins gE and gB are internalized
from the plasma membrane of cells, while gI and gC are not internalized
efficiently. We show for gE that the cytoplasmic domain of the protein
is required for endocytosis. While the gI protein is incapable of
endocytosis on its own, it can be internalized when complexed with gE.
We demonstrate that endocytosis of the gE-gI complex and gB occurs early after infection of tissue culture cells but that this process stops completely after 6 h of infection, a time that correlates with significant shutoff of host protein synthesis. We also show that
gE protein internalized at 4 h postinfection is not present in
virions formed at a later time. We discuss the differences in PRV gE
and gI endocytosis compared to that of the varicella-zoster virus
homologs and the possible roles of glycoprotein endocytosis in the
virus life cycle.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Role of Envelope Protein gE Endocytosis in
the Pseudorabies Virus Life Cycle
*
Corresponding author. Mailing address: Department of
Molecular Biology, Princeton University, Princeton, NJ 08544. Phone: (609) 258-2415. Fax: (609) 258-1035. E-mail:
Lenquist{at}molbiol.princeton.edu.
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