Identification of Marek's Disease Virus VP22 Tegument Protein Domains Essential for Virus Cell-to-Cell Spread, Nuclear Localization, Histone Association and Cell-Cycle Arrest

Autor: G. Le Pape, Caroline Denesvre, Fabien Loustalot, Sylvie Rémy, Katia Courvoisier, Laëtitia Trapp-Fragnet
Přispěvatelé: Infectiologie et Santé Publique (UMR ISP), Institut National de la Recherche Agronomique (INRA)-Université de Tours (UT), INRA subventions, Trapp-Fragnet, Laëtitia, Denesvre, Caroline, Institut National de la Recherche Agronomique (INRA)-Université de Tours
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Cell cycle checkpoint
animal diseases
Mardivirus
viruses
lcsh:QR1-502
Virus Replication
lcsh:Microbiology
Alphaherpesvirus
Marek’s disease virus
VP22
cell cycle
functional domains
histones
subcellular localization
virus spread
Sequence Analysis
Protein

hemic and lymphatic diseases
0303 health sciences
Microbiology and Parasitology
virus diseases
Cell cycle
Microbiologie et Parasitologie
3. Good health
Cell biology
Infectious Diseases
Histone
[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology
virus maladie de marek
Gene Expression Regulation
Viral

Protein domain
cytométrie de flux
Biology
Virus
Article
03 medical and health sciences
Viral Proteins
Protein Domains
Virology
Marek Disease
Animals
Amino Acid Sequence
Gene
Herpesvirus 2
Gallid

030304 developmental biology
Cell Nucleus
Viral Structural Proteins
Marek's disease
030306 microbiology
génome
Cell Cycle Checkpoints
biochemical phenomena
metabolism
and nutrition

biology.organism_classification
cycle cellulaire
DNA
Viral

biology.protein
Chickens
Zdroj: Viruses
Viruses, MDPI, 2019, 11 (6), 22 p. ⟨10.3390/v11060537⟩
Viruses, Vol 11, Iss 6, p 537 (2019)
Volume 11
Issue 6
Viruses 6 (11), 1-23. (2019)
ISSN: 1999-4915
DOI: 10.3390/v11060537⟩
Popis: VP22 is a major tegument protein of alphaherpesviruses encoded by the UL49 gene. Two properties of VP22 were discovered by studying Marek&rsquo
s disease virus (MDV), the Mardivirus prototype
it has a major role in virus cell-to-cell spread and in cell cycle modulation. This 249 AA-long protein contains three regions including a conserved central domain. To decipher the functional VP22 domains and their relationships, we generated three series of recombinant MDV genomes harboring a modified UL49 gene and assessed their effect on virus spread. Mutated VP22 were also tested for their ability to arrest the cell cycle, subcellular location and histones copurification after overexpression in cells. We demonstrated that the N-terminus of VP22 associated with its central domain is essential for virus spread and cell cycle modulation. Strikingly, we demonstrated that AAs 174-190 of MDV VP22 containing the end of a putative extended alpha-3 helix are essential for both functions and that AAs 159&ndash
162 located in the putative beta-strand of the central domain are mandatory for cell cycle modulation. Despite being non-essential, the 59 C-terminal AAs play a role in virus spread efficiency. Interestingly, a positive correlation was observed between cell cycle modulation and VP22 histones association, but none with MDV spread.
Databáze: OpenAIRE