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Journal of Virology, October 2004, p. 10449-10459, Vol. 78, No. 19
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.19.10449-10459.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

In Vivo Function of a Gammaherpesvirus Virion Glycoprotein: Influence on B-Cell Infection and Mononucleosis

James P. Stewart,1* Ondine J. Silvia,2 Isobel M. D. Atkin,2 David J. Hughes,1 Bahram Ebrahimi,1 and Heiko Adler3

Centre for Comparative Infectious Diseases, Department of Medical Microbiology, University of Liverpool, Liverpool,1 Department of Veterinary Pathology, University of Edinburgh, Edinburgh, United Kingdom,2 Institute for Molecular Immunology, Clinical Cooperation Group Hematopoietic Cell Transplantation, GSF-Research Center for Environment and Health, Munich, Germany3

Received 26 November 2003/ Accepted 19 May 2004

The human gammaherpesviruses Epstein-Barr virus and Kaposi Sarcoma-associated herpesvirus both contain a glycoprotein (gp350/220 and K8.1, respectively) that mediates binding to target cells and has been studied in great detail in vitro. However, there is no direct information on the role that these glycoproteins play in pathogenesis in vivo. Infection of mice by murid herpesvirus 4 strain 68 (MHV-68) is an established animal model for gammaherpesvirus pathogenesis and expresses an analogous glycoprotein, gp150. To elucidate the in vivo function of gp150, a recombinant MHV-68 deficient in gp150 production was generated (vgp150{Delta}). The productive viral replication in vitro and in vivo was largely unaffected by mutation of gp150, aside from a partial defect in the release of extracellular virus. Likewise, B-cell latency was established. However, the transient mononucleosis and spike in latently infected cells associated with the spread of MHV-68 to the spleen was significantly reduced in vgp150{Delta}-infected mice. A soluble, recombinant gp150 was found to bind specifically to B cells but not to epithelial cells in culture. In addition, gp150-deficient MHV-68 derived from mouse lungs bound less well to spleen cells than wild-type virus. Thus, gp150 is highly similar in function in vitro to the Epstein-Barr virus gp350/220. These results suggest a role for these analogous proteins in mononucleosis and have implications for their use as vaccine antigens.

* Corresponding author. Mailing address: Department of Medical Microbiology, University of Liverpool, Duncan Building, Daulby St., Liverpool L69 3GA, United Kingdom. Phone: 44-151-794-7596. Fax: 44-151-706-5805. E-mail: j.p.stewart{at}liv.ac.uk.

Journal of Virology, October 2004, p. 10449-10459, Vol. 78, No. 19
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.19.10449-10459.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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