Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person Based on mass spectroscopy of purified viral particles of hu...
| Class:Id | Summation:9836099 |
|---|---|
| _displayName | Based on mass spectroscopy of purified viral particles of hu... |
| _timestamp | 2023-06-27 04:14:06 |
| created | [InstanceEdit:9836098] Orlic-Milacic, Marija, 2023-05-22 |
| literatureReference | [LiteratureReference:9835154] Protein analysis of purified respiratory syncytial virus particles reveals an important role for heat shock protein 90 in virus particle assembly [LiteratureReference:9836154] Helical ordering of envelope-associated proteins and glycoproteins in respiratory syncytial virus [URL:9836284] https://doi.org/10.1101/2021.10.13.464285 [LiteratureReference:9836378] A Proteomic-Based Workflow Using Purified Respiratory Syncytial Virus Particles to Identify Cellular Factors as Drug Targets [LiteratureReference:9837633] Architecture of respiratory syncytial virus revealed by electron cryotomography [LiteratureReference:9825347] Crystal structure of a nucleocapsid-like nucleoprotein-RNA complex of respiratory syncytial virus [LiteratureReference:9823510] The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer [LiteratureReference:9838858] Sequencing and analysis of globally obtained human respiratory syncytial virus A and B genomes |
| modified | [InstanceEdit:9836157] Orlic-Milacic, Marija, 2023-05-24 [InstanceEdit:9836288] Orlic-Milacic, Marija, 2023-05-25 [InstanceEdit:9836380] Orlic-Milacic, Marija, 2023-05-27 [InstanceEdit:9837634] Orlic-Milacic, Marija, 2023-06-16 [InstanceEdit:9838877] Orlic-Milacic, Marija, 2023-06-27 [InstanceEdit:9838878] Orlic-Milacic, Marija, 2023-06-27 |
| text | 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). |
| (summation) | [BlackBoxEvent:9835171] Budding of hRSV A virions from infected cell [Homo sapiens] |
| [Change default viewing format] | |
No pathways have been reviewed or authored by Based on mass spectroscopy of purified viral particles of hu... (9836099)
