Based on mass spectroscopy of purified viral particles of hu...

created [InstanceEdit:9836098] Orlic-Milacic, Marija, 2023-05-22
dbId 9836100
displayName Based on mass spectroscopy of purified viral particles of hu...
literatureReference
modified [InstanceEdit:9838875] Orlic-Milacic, Marija, 2023-06-27
schemaClass Summation
text Based on mass spectroscopy of purified viral particles of human respiratory syncytial virus (RSV) A2, the ratio of matrix protein M to nucleocapsid protein N is ~1:1 (Radhakrishnan et al. 2010). Based on the curatorial estimation that viral genomic RNA is packaged around 209 oligomeric rings of N protein, of which 129 are N decamers (10 N subunits) and 80 are N hendecamers (11 N subunits), and taking into consideration the experimentally determined length of RSV genomic RNA (Bose et al. 2015), number of genomic RNA nucleotides bound by each N subunit (Tawar et al. 2009), and the ratio of N decamers to N hendecamers in RSV nucleocapsids (Tran et al. 2007), the total number of N proteins in a viral nucleocapsid is expected to be 2170. As M protein forms dimers, which are a prerequisite for further oligomerization during matrix lattice formation as well as formation of viral filaments and viral budding (Förster et al. 2015), we are showing that 1085 M dimers are involved in formation of the matrix lattice around the nucleocapsid.

Virion assembly occurs in cytoplasmic inclusion bodies localized in the vicinity of the plasma membrane region where virus filaments, which represent budding virions, form. Each infected cell usually contains several viral inclusion bodies of irregular shape and varying sizes (Radhakrishnan et al. 2010).

Based on cryogenic electron microscopy (cryoEM) and cryogenic electron tomography (cryoET), M protein dimers form a helical lattice that constitutes an endoskeleton under the viral envelope (Conley et al. 2022; Sibert et al. 2021).
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