<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Machiels, Bénédicte</style></author><author><style face="normal" font="default" size="100%">Lété, Céline</style></author><author><style face="normal" font="default" size="100%">Guillaume Antoine</style></author><author><style face="normal" font="default" size="100%">Jan Mast</style></author><author><style face="normal" font="default" size="100%">Stevenson, Philip G</style></author><author><style face="normal" font="default" size="100%">Vanderplasschen, Alain</style></author><author><style face="normal" font="default" size="100%">Gillet, Laurent</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Antibody evasion by a gammaherpesvirus O-glycan shield.</style></title><secondary-title><style face="normal" font="default" size="100%">PLoS Pathog</style></secondary-title><alt-title><style face="normal" font="default" size="100%">PLoS Pathog.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Epitopes</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycosylation</style></keyword><keyword><style  face="normal" font="default" size="100%">Herpesvirus 4, Bovine</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Glycoproteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Neutralization Tests</style></keyword><keyword><style  face="normal" font="default" size="100%">Rabbits</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Alignment</style></keyword><keyword><style  face="normal" font="default" size="100%">Viral Envelope Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Virion</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Replication</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2011 Nov</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">e1002387</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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 glycan shield for otherwise vulnerable viral epitopes. Interestingly, this O-glycan shield could be exploited for neutralization by lectins and carbohydrate-specific antibody. The conservation of O-glycosylation sites in all gp350 homologs suggests that this is a general evasion mechanism that may also provide a therapeutic target.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">11</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/22114560?dopt=Abstract</style></custom1></record></records></xml>