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 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.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Machiels B,Lété C,Guillaume A,Mast J,Stevenson PG,Vanderplasschen A,Gillet Ldoi
10.1371/journal.ppat.1002387subject
Has Abstractpub_date
2011-11-01 00:00:00pages
e1002387issue
11eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-11-00324journal_volume
7pub_type
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