Budding of hRSV A virions from infected cell

Stable Identifier
R-HSA-9835171
Type
Reaction [omitted]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
plasma membrane
ReviewStatus
5/5
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Budding of hRSV A virions from infected cell
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Based on mass spectroscopy of purified viral particles of human respiratory syncytial virus (RSV) A2, the ratio of fusion protein F to nucleocapsid protein N is ~3:4, while the ratio of mature glycoprotein G to F protein is ~1:30. This low G to F ratio could, however, be due to the hydrophobic nature of the G protein, which makes its recovery difficult, as well its heavy glycosylation, which interferes with peptide identification by mass spectroscopy (Radhakrishnan et al. 2010). In the same study, the SH protein was not detected, which may also have been a consequence of SH being highly hydrophobic.

In this reaction, we are showing SH protein in ~1:1 ratio with the G protein. 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 considerations 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 the F protein forms trimers, and SH protein forms pentamers, we are showing that 542 F trimers, 54 G proteins, and 10 SH protein pentamers become embedded in the virion membrane.

Budding virions are observed as viral filaments at the plasma membrane of infected cells. Viral filaments are connected with cytoplasmic inclusion bodies where the virion assembly occurs. Viral nucleocapsids appear as strands along the length of viral filaments, with some viral filaments containing more than one viral nucleocapsid (Radhakrishnan et al. 2010; Liljeroos et al. 2013; Conley et al. 2022).

Based on cryogenic electron microscopy (cryoEM) and cryogenic electron tomography (cryoET), glycoproteins that stud the viral envelope are clustered in pairs and helically ordered; an organization that is coordinated by the M protein lattice (Conley et al. 2022; Liljeroos et al. 2013; Sibert et al. 2021).

The cortical actin network takes part in formation of viral filaments. In particular, the association of beta-actin (ACTB), filamin-1 (FLNA), and cofilin-1(CFL1) with viral filaments has been confirmed (Radhakrishnan et al. 2010, Huong et al. 2016). HSP90A is needed for formation of mature virions and both isoforms of HSP90A (HSP90AA1, and HSP90AB1) can be found as components of viral filaments (Radhakrishnan et al. 2010).
Literature References
PubMed ID Title Journal Year
27464695 A Proteomic-Based Workflow Using Purified Respiratory Syncytial Virus Particles to Identify Cellular Factors as Drug Targets

Tan, BH, Sugrue, RJ, Huong, TN

Methods Mol Biol 2016
34935163 Helical ordering of envelope-associated proteins and glycoproteins in respiratory syncytial virus

Stewart, M, Conley, MJ, Haney, J, Hutchings, J, Zanetti, G, Fearns, R, Streetley, J, Bhella, D, Vijayakrishnan, S, Jaffery, H, Power, BJ, Burns, AM, Bakker, SE, Short, JM, Murcia, PR

EMBO J 2022
  Respiratory syncytial virus matrix protein assembles as a lattice with local and extended order that coordinates the position of the fusion glycoprotein

Sibert, BS, Ke, Z, Stobart, CC, Kim, JY, Wright, ER, Moore, MM, Yang, JE

   
23776214 Architecture of respiratory syncytial virus revealed by electron cryotomography

Krzyzaniak, MA, Helenius, A, Butcher, SJ, Liljeroos, L

Proc Natl Acad Sci U S A 2013
20530633 Protein analysis of purified respiratory syncytial virus particles reveals an important role for heat shock protein 90 in virus particle assembly

Radhakrishnan, A, Iyer, LR, Tan, BH, Tang, K, Fleck, R, Sugrue, RJ, Yarwood, A, Yeo, D, Brink, J, Myaing, MZ, Sanmun, D, Brown, G, Aitken, J

Mol Cell Proteomics 2010
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Authored
Orlic-Milacic, M  (2023-05-11)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Orlic-Milacic, M  (2023-05-11)
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