Article (Scientific journals)
Antibody evasion by a gammaherpesvirus o-glycan shield.
Machiels, Bénédicte; Lété, Céline; Guillaume, Antoine et al.
2011In PLoS Pathogens, 7 (11), p. 1002387
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Abstract :
[en] 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.
Disciplines :
Microbiology
Author, co-author :
Machiels, Bénédicte  ;  Université de Liège - ULiège > Immunologie et vaccinologie
Lété, Céline ;  Université de Liège - ULiège > Immunologie et vaccinologie
Guillaume, Antoine ;  Université de Liège - ULiège > Immunologie et vaccinologie
Mast, Jan
Stevenson, Philip G
Vanderplasschen, Alain ;  Université de Liège - ULiège > Immunologie et vaccinologie
Gillet, Laurent  ;  Université de Liège - ULiège > Immunologie et vaccinologie
Language :
English
Title :
Antibody evasion by a gammaherpesvirus o-glycan shield.
Publication date :
2011
Journal title :
PLoS Pathogens
ISSN :
1553-7366
eISSN :
1553-7374
Publisher :
Public Library of Science, San Francisco, United States - California
Volume :
7
Issue :
11
Pages :
e1002387
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 04 January 2012

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