Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

ABSTRACT: Stabilization of the SARS-CoV-2 receptor binding domain by protein core redesign and deep mutational scanning

PROVIDER: PRJNA797453 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR17623152_1.fastq.gz	Fastqsanger.gz
	SRR17623152_2.fastq.gz	Fastqsanger.gz
	SRR17623153_1.fastq.gz	Fastqsanger.gz
	SRR17623153_2.fastq.gz	Fastqsanger.gz
	SRR17623154_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 32

Similar Datasets

Severe acute respiratory syndrome coronavirus 2

Project description:Deep mutational scanning of SARS-CoV-2 Spike N-terminal domain (NTD)

| PRJNA792013 | ENA

Severe acute respiratory syndrome coronavirus 2

Project description:Deep mutational scanning of SARS-CoV-2 Spike HR1

| PRJNA826665 | ENA

Project description:Deep mutational scanning of SARS-CoV-2 3CL protease

| PRJNA813935 | ENA

An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants

Project description:The spike S of SARS-CoV-2 recognizes ACE2 on the host cell membrane to initiate entry. Soluble decoy receptors, in which the ACE2 ectodomain is engineered to block S with high affinity, potently neutralize infection and, due to close similarity with the natural receptor, hold out the promise of being broadly active against virus variants without opportunity for escape. Here, we directly test this hypothesis. Using deep mutagenesis, we find that the ACE2-binding surface of the SARS-CoV-2 spike tolerates high mutational diversity, which may act as a source for resistance to therapeutics. However, saturation mutagenesis of the receptor-binding domain (RBD) followed by in vitro selection, with wild type ACE2 and the engineered decoy competing for binding sites, failed to find S mutants that discriminate in favor of the wild type receptor. We conclude that resistance to engineered decoys will be rare.

2020-10-18 | GSE159372 | GEO

The sequence of human ACE2 is suboptimal for binding the S spike protein of SARS coronavirus 2

Project description:The rapid and escalating spread of SARS coronavirus 2 (SARS-CoV-2) poses an immediate public health emergency, and no approved therapeutics or vaccines are currently available. The viral spike protein S binds membrane-tethered ACE2 on host cells in the lungs to initiate molecular events that ultimately release the viral genome intracellularly. The extracellular protease domain of ACE2 inhibits cell entry of both SARS and SARS-2 coronaviruses by acting as a soluble decoy for receptor binding sites on S, and is a promising candidate for therapeutic and prophylactic development. Using deep mutagenesis, variants of ACE2 are identified with increased binding to the receptor binding domain of S at a cell surface. Mutations are found across the protein-protein interface and also at buried sites where they are predicted to enhance folding and presentation of the interaction epitope. The mutational landscape offers a preliminary blueprint for engineering high affinity ACE2 receptors to meet this unprecedented challenge.

2020-03-19 | GSE147194 | GEO

Project description:Deep mutational scanning of SARS-CoV-2 spike fusion peptide

| PRJNA910585 | ENA

The PDZ-binding motif of SARS-CoV envelope protein is a determinant of viral pathogenesis

Project description:A recombinant SARS-CoV lacking the envelope (E) protein is attenuated in vivo. Here we report that E protein PDZ-binding motif (PBM), a domain involved in protein-protein interactions, is a major virulence determinant in vivo. Elimination of SARS-CoV E protein PBM by using reverse genetics led to attenuated viruses (SARS-CoV-mutPBM) and to a reduction in the deleterious exacerbate immune response triggered during infection with the parental virus (SARS-CoV-wt). Cellular protein syntenin bound E protein PBM during SARS-CoV infection. Syntenin activates p38 MAPK leading to overexpression of inflammatory cytokines, and we have shown that active p38 MAPK was reduced in lungs of mice infected with SARS-CoVs lacking E protein PBM (SARS-CoV-mutPBM) as compared with the parental virus (SARS-CoV-wt), leading to a decreased expression of inflammatory cytokines and to viral attenuation. Therefore, E protein PBM is a virulence factor that activates pathogenic immune response most likely by using syntenin as a mediator of p38 MAPK induced inflammation. Three biological replicates were independently hybridized (one channel per slide) for each sample type (SARS-CoV-wt, SARS-CoV-mutPBM, Mock). Slides were Sure Print G3 Agilent 8x60K Mouse (G4852A-028005)

2014-10-31 | E-GEOD-52920 | biostudies-arrayexpress

SARS-CoV-2 pseudovirus strain:BA.2

Project description:SARS-CoV-2 BA.2 spike pseudovirus-based deep mutational scanning

| PRJNA1035933 | ENA

Project description:SARS-CoV-2 spike phage deep mutational scanning to map binding residues of monoclonal antibodies

| PRJNA1130943 | ENA

Project description:SARS-CoV-2 spike phage deep mutational scanning to map binding residues of monoclonal antibodies

| PRJNA1122188 | ENA