antibody evasion by a gammaherpesvirus o-glycan shield抗体由gammaherpesvirus逃税o-glycan盾牌.pdfVIP

Antibody Evasion by a Gammaherpesvirus O-Glycan Shield ´ ´ 1 ´ ´ ´ 1 1 2 3 Benedicte Machiels , Celine Lete , Antoine Guillaume , Jan Mast , Philip G. Stevenson , Alain 1 1 Vanderplasschen , Laurent Gillet * ` ` 1 Immunology-Vaccinology (B43b), Department of Infectious and Parasitic Diseases (B43b), Faculty of Veterinary Medicine, University of Liege, Liege, Belgium, 2 Department Biocontrole, Research Unit Electron Microscopy, Veterinary and Agrochemical Research Centre, CODA-CERVA, Groeselenberg, Ukkel, Belgium, 3 Division of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom Abstract All gammaherpesviruses encode a major glycoprotein homologous to the Epstein-Barr virus gp350. These glycoproteins are often involved in cell binding, and some provide neutralization targets. However, the capacity of gammaherpesviruses for long-term transmission from immune hosts implies that in vivo neutralization is incomplete. In this study, we used Bovine Herpesvirus 4 (BoHV-4) to determine how its gp350 homolog - gp180 - contributes to virus replication and neutralization. A lack of gp180 had no impact on the establishment and maintenance of BoHV-4 latency, but markedly sensitized virions to neutralization by immune sera. Antibody had greater access to gB, gH and gL on gp180-deficient virions, including neutralization epitopes. Gp180 appears to be highly O-glycosylated, and removing O-linked glycans from virions also sensitized them to neutralization. It therefore appeared that gp180 provides part of a