title: Proteomic characterization of murid herpesvirus 4 extracellular virions.
abstract: Gammaherpesvirinae, such as the human Epstein-Barr virus (EBV) and the Kaposi's sarcoma associated herpesvirus (KSHV) are highly prevalent pathogens that have been associated with several neoplastic diseases. As EBV and KSHV are host-range specific and replicate poorly in vitro, animal counterparts such as Murid herpesvirus-4 (MuHV-4) have been widely used as models. In this study, we used MuHV-4 in order to improve the knowledge about proteins that compose gammaherpesviruses virions. To this end, MuHV-4 extracellular virions were isolated and structural proteins were identified using liquid chromatography tandem mass spectrometry-based proteomic approaches. These analyses allowed the identification of 31 structural proteins encoded by the MuHV-4 genome which were classified as capsid (8), envelope (9), tegument (13) and unclassified (1) structural proteins. In addition, we estimated the relative abundance of the identified proteins in MuHV-4 virions by using exponentially modified protein abundance index analyses. In parallel, several host proteins were found in purified MuHV-4 virions including Annexin A2. Although Annexin A2 has previously been detected in different virions from various families, its role in the virion remains controversial. Interestingly, despite its relatively high abundance in virions, Annexin A2 was not essential for the growth of MuHV-4 in vitro. Altogether, these results extend previous work aimed at determining the composition of gammaherpesvirus virions and provide novel insights for understanding MuHV-4 biology.
authors.affiliation: Department of Infectious Diseases, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
authors.forename: Sarah
authors.initials: S
authors.lastname: Vidick
authors.affiliation: Department of Proteomics and Microbiology, Research Institute for Biosciences Interdisciplinary Mass Spectrometry Center (CISMa), University of Mons, Mons, Belgium.
authors.forename: Baptiste
authors.initials: B
authors.lastname: Leroy
authors.affiliation: Department of Infectious Diseases, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
authors.forename: Leonor
authors.initials: L
authors.lastname: Palmeira
authors.affiliation: Department of Infectious Diseases, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
authors.forename: Bénédicte
authors.initials: B
authors.lastname: Machiels
authors.affiliation: Electron Microscopy Unit, Veterinary and Agrochemical Research Centre, Brussels, Belgium.
authors.forename: Jan
authors.initials: J
authors.lastname: Mast
authors.affiliation: Department of Infectious Diseases, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
authors.forename: Sylvie
authors.initials: S
authors.lastname: François
authors.affiliation: Department of Proteomics and Microbiology, Research Institute for Biosciences Interdisciplinary Mass Spectrometry Center (CISMa), University of Mons, Mons, Belgium.
authors.forename: Ruddy
authors.initials: R
authors.lastname: Wattiez
authors.affiliation: Department of Infectious Diseases, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
authors.forename: Alain
authors.initials: A
authors.lastname: Vanderplasschen
authors.affiliation: Department of Infectious Diseases, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
authors.forename: Laurent
authors.initials: L
authors.lastname: Gillet
mesh_terms: D000818:Animals; D002213:Capsid / Q000378:metabolism; D002460:Cell Line; D006224:Cricetinae; D005110:Extracellular Space / Q000821:virology*; D006031:Glycosylation; D013058:Mass Spectrometry; D040901:Proteomics; D018144:Rhadinovirus / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism; D014771:Virion / Q000378:metabolism*
chemical_list: D014764:Viral Proteins