Last update 01 Nov 2024

SARS-CoV-2 S protein x RSV F protein

Last update 01 Nov 2024

Basic Info

Related Targets

SARS-CoV-2 S proteinRSV F protein

Drugs associated with SARS-CoV-2 S protein x RSV F protein

SF-LNP

Target

RSV F protein x SARS-CoV-2 S protein

Mechanism

Respiratory syncytial virus F protein inhibitors [+1]

Active Org.

University of Science & Technology of China

Originator Org.

China University of Technology

Active Indication

COVID-19 [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SARS-CoV-2 S protein x RSV F protein

100 Translational Medicine associated with SARS-CoV-2 S protein x RSV F protein

0 Patents (Medical) associated with SARS-CoV-2 S protein x RSV F protein

Literatures (Medical) associated with SARS-CoV-2 S protein x RSV F protein

17 Oct 2017·Proceedings of the National Academy of SciencesQ1 · CROSS-FIELD

Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion

Q1 · CROSS-FIELD

Article

Author: Bosch, Berend-Jan ; Snijder, Joost ; Tortorici, M. Alejandra ; Walls, Alexandra C. ; Veesler, David ; Rey, Felix A. ; Xiong, Xiaoli

SignificanceThe pandemic potential of coronaviruses was recently demonstrated twice by global outbreaks of deadly pneumonia. The spike (S) glycoprotein initiates infection through conformational changes that remain largely uncharacterized. Here we report the cryoEM structure of an S glycoprotein in the postfusion state, showing large-scale rearrangements compared with the prefusion trimer. We further characterized the refolding of the metastable prefusion conformation using limited proteolysis, mass spectrometry, and single-particle EM. The observed similarity to paramyxovirus F structures demonstrates a conserved refolding trajectory and supports the evolutionary relatedness of their fusion subunits. Finally, our data provide a structural framework for understanding antibody neutralization and for engineering vaccines against this medically important virus family.

PLoS ONEQ3 · CROSS-FIELD

Critical Role of the Fusion Protein Cytoplasmic Tail Sequence in Parainfluenza Virus Assembly

Q3 · CROSS-FIELD

ArticleOA

Author: Raychel Stone ; Toru Takimoto

Interactions between viral glycoproteins, matrix protein and nucleocapsid sustain assembly of parainfluenza viruses at the plasma membrane. Although the protein interactions required for virion formation are considered to be highly specific, virions lacking envelope glycoprotein(s) can be produced, thus the molecular interactions driving viral assembly and production are still unclear. Sendai virus (SeV) and human parainfluenza virus type 1 (hPIV1) are highly similar in structure, however, the cytoplasmic tail sequences of the envelope glycoproteins (HN and F) are relatively less conserved. To unveil the specific role of the envelope glycoproteins in viral assembly, we created chimeric SeVs whose HN (rSeVhHN) or HN and F (rSeVh(HN+F)) were replaced with those of hPIV1. rSeVhHN grew as efficiently as wt SeV or hPIV1, suggesting that the sequence difference in HN does not have a significant impact on SeV replication and virion production. In sharp contrast, the growth of rSeVh(HN+F) was significantly impaired compared to rSeVhHN. rSeVh(HN+Fstail) which expresses a chimeric hPIV1 F with the SeV cytoplasmic tail sequence grew similar to wt SeV or rSeVhHN. Further analysis indicated that the F cytoplasmic tail plays a critical role in cell surface expression/accumulation of HN and F, as well as NP and M association at the plasma membrane. Trafficking of nucelocapsids in infected cells was not significantly affected by the origin of F, suggesting that F cytoplasmic tail is not involved in intracellular movement. These results demonstrate the role of the F cytoplasmic tail in accumulation of structural components at the plasma membrane assembly sites.

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