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Journal of Virology, June 2005, p. 7248-7254, Vol. 79, No. 11
0022-538X/05/$08.00+0 doi:10.1128/JVI.79.11.7248-7254.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Laboratory of Virology,1 Laboratory of Immunology, Faculty of Veterinary Medicine, Ghent University, Merelbeke, Belgium,2 Department of Molecular Virology, Faculty of Biotechnology, Gdansk University, Gdansk, Poland3
Received 24 January 2005/ Accepted 9 February 2005
Viral glycoproteins gB and gD of the swine alphaherpesvirus pseudorabies virus (PRV), which is closely related to human herpes simplex virus and varicella-zoster virus, are able to drive internalization of antibody-antigen complexes that may form at the cell surface of infected monocytes, thereby protecting these cells from efficient antibody-mediated lysis. We found earlier that gB relies on an endocytosis motif in its cytoplasmic domain for its function during this internalization process. Here, we report that the PRV gD protein also contains a functional endocytosis motif (YRLL) in its cytoplasmic domain that drives spontaneous endocytosis of gD from the cell surface early in infection and that acts in concert with the endocytosis motif in gB to contribute to efficient internalization of antibody-antigen complexes in PRV-infected monocytes.
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