Reference : Proteomic characterization of bovine herpesvirus 4 extracellular virions.
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/135280
Proteomic characterization of bovine herpesvirus 4 extracellular virions.
English
Lété, Céline mailto [Université de Liège - ULg > > Immunologie et vaccinologie >]
Palmeira, Leonor [Université de Liège - ULg > > Immunologie et vaccinologie >]
Leroy, Baptiste [> >]
Mast, Jan [> >]
Machiels, Bénédicte mailto [Université de Liège - ULg > > Immunologie et vaccinologie >]
Wattiez, Ruddy [> >]
Vanderplasschen, Alain mailto [Université de Liège - ULg > > Immunologie et vaccinologie >]
Gillet, Laurent mailto [Université de Liège - ULg > > Immunologie et vaccinologie >]
2012
Journal of Virology
86
21
11567-80
Yes (verified by ORBi)
International
0022-538X
1098-5514
United States
[en] Gammaherpesviruses are important pathogens in human and animal populations. During early events of infection, these viruses manipulate preexisting host cell signaling pathways to allow successful infection. The different proteins that compose viral particles are therefore likely to have critical functions not only in viral structures and in entry into target cell but also in evasion of the host's antiviral response. In this study, we analyzed the protein composition of bovine herpesvirus 4 (BoHV-4), a close relative of the human Kaposi's sarcoma-associated herpesvirus. Using mass spectrometry-based approaches, we identified 37 viral proteins associated with extracellular virions, among which 24 were resistant to proteinase K treatment of intact virions. Analysis of proteins associated with purified capsid-tegument preparations allowed us to define protein localization. In parallel, in order to identify some previously undefined open reading frames, we mapped peptides detected in whole virion lysates onto the six frames of the BoHV-4 genome to generate a proteogenomic map of BoHV-4 virions. Furthermore, we detected important glycosylation of three envelope proteins: gB, gH, and gp180. Finally, we identified 38 host proteins associated with BoHV-4 virions; 15 of these proteins were resistant to proteinase K treatment of intact virions. Many of these have important functions in different cellular pathways involved in virus infection. This study extends our knowledge of gammaherpesvirus virions composition and provides new insights for understanding the life cycle of these viruses.
http://hdl.handle.net/2268/135280

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
BoHV-4 proteomic.pdfPublisher postprint2.04 MBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.