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Journal of Virology, July 2002, p. 6845-6851, Vol. 76, No. 13
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.13.6845-6851.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

A Tyrosine-Based Motif in the Cytoplasmic Tail of Pseudorabies Virus Glycoprotein B Is Important for both Antibody-Induced Internalization of Viral Glycoproteins and Efficient Cell-to-Cell Spread

Herman W. Favoreel,1,2 Geert Van Minnebruggen,1 Hans J. Nauwynck,1* Lynn W. Enquist,2 and Maurice B. Pensaert1

Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Merelbeke, Belgium,1 Department of Molecular Biology, Princeton University, Princeton, New Jersey2

Received 18 December 2001/ Accepted 25 January 2002

Pseudorabies virus (PRV), a swine alphaherpesvirus, is capable of causing viremia in vaccinated animals. Two mechanisms that may help PRV avoid recognition by the host immune system during this viremia are direct cell-to-cell spread in tissue and antibody-induced internalization of viral cell surface glycoproteins in PRV-infected blood monocytes, the carrier cells of the virus in the blood. PRV glycoprotein B (gB) is crucial during both processes. Here we show that mutating a tyrosine residue located in a YXX{Phi} motif in the gB cytoplasmic tail results in decreased efficiency of cell-to-cell spread and a strong reduction in antibody-induced internalization of viral cell surface glycoproteins. Mutating the dileucine motif in the gB tail led to an increased cell-to-cell spread of the virus and the formation of large syncytia.

* Corresponding author. Mailing address: Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium. Phone: 32 (0)9 264 73 73. Fax: 32 (0)9 264 74 95. E-mail: Hans.Nauwynck{at}rug.ac.be.

Journal of Virology, July 2002, p. 6845-6851, Vol. 76, No. 13
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.13.6845-6851.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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