Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

ABSTRACT: Deep mutational scanning of the influenza A virus nonstructural protein 2 (NS2)

PROVIDER: PRJNA1083715 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR28221591_1.fastq.gz	Fastqsanger.gz
	SRR28221591_2.fastq.gz	Fastqsanger.gz
	SRR28221592_1.fastq.gz	Fastqsanger.gz
	SRR28221592_2.fastq.gz	Fastqsanger.gz
	SRR28221593_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 8

Similar Datasets

Efficient genome replication in influenza A virus requires NS2 and sequence beyond the canonical promoter

Project description:Influenza A virus encodes promoters in both the sense and antisense orientations. These support the generation of new genomes, antigenomes, and mRNA transcripts. Characterization of the influenza promoters using minimal replication assays—transfections with viral polymerase, nucleoprotein, and a genomic template—defined their sequence as 13nt at the 5’ end of the viral genomic RNA (U13) and 12nt at the 3’ end (U12).Other than a single position the U12 and U13 sequences are identical between all eight RNA molecules that comprise the segmented influenza genome.Nevertheless, each segment can exhibit different transcriptional dynamics despite possessing identical promoters.Minimal replication assays lack the influenza protein NS2, which can modulate transcription and replication differentially between influenza segments.This suggests that NS2 expression may redefine the influenza A virus promoter.In this work we assess how internal regions of sequence in two genomic segments, HA and PB1, may contribute to NS2-dependent replication as well as map such interactions down to individual nucleotides in PB1. We find that the expression of NS2 significantly alters sequence requirements for efficient replication beyond the identical U12 and U13 sequence, providing a mechanism for the divergent replication and transcription dynamics across the influenza A virus genome.

2024-09-10 | GSE276697 | GEO

Project description:Deep mutational scanning of influenza H3N2 neuraminidase

| PRJNA857746 | ENA

Influenza A virus

Project description:Deep mutational scanning of influenza H3 HA

| PRJNA1124381 | ENA

Saccharomyces cerevisiae

Project description:Deep mutational scanning of an ancestral protein

| PRJNA362734 | ENA

Henipavirus nipahense

Project description:Deep mutational scanning of the Nipah virus receptor binding protein (RBP)

| PRJNA1194132 | ENA

Project description:Deep mutational scanning of the CVB3 capsid protein

| PRJNA643896 | ENA

Project description:Deep mutational scanning of E. coli protein EnvZ

| PRJNA902002 | ENA

ER proteostasis and temperature differentially impact the mutational tolerance of influenza hemagglutinin

Project description:Here, we present a systematic and quantitative test of the hypothesis that the composition and activities of the endoplasmic reticulum (ER) proteostasis network impact mutational tolerance of secretory pathway client proteins. We focus on influenza hemagluttinin (HA), a viral coat protein that folds in the host’s ER via a complex but well-characterized pathway. By integrating chemical methods to modulate the unfolded protein response with deep mutational scanning to assess mutational tolerance, we discover that upregulation of ER chaperones broadly enhances HA mutational tolerance across numerous sites and secondary/tertiary structure elements, including sites targeted by host antibodies. Remarkably, this host chaperone-enhanced mutational tolerance is observed at the same HA sites where mutational tolerance is most reduced by propagation at a fever-like temperature. Thus, host ER proteostasis mechanisms and temperature modulate HA mutational tolerance in opposite directions. This finding has important implications for influenza evolution, because influenza immune escape is contingent on HA possessing sufficient mutational tolerance to acquire antibody resistance while still maintaining the capacity to fold and function. More broadly, this work provides the first experimental evidence that the composition and activities of the ER proteostasis network critically define the mutational tolerance and, therefore, the evolution of secretory pathway client proteins.

2018-09-10 | GSE115168 | GEO

Project description:In vivo deep mutational scanning and drug resistance profiling of Influenza A virus neuraminidase

| PRJNA801090 | ENA

The influenza B virus hemagglutinin head domain is less tolerant to transposon mutagenesis than that of the influenza A virus

Project description:To determine if the influenza B virus HA is under constraints that limit its antigenic variation, we performed a transposon screen to compare the mutational tolerance of the currently circulating influenza A virus HAs (H1 and H3 subtypes) and influenza B virus HAs (B/Victoria87 and B/Yamagata88 antigenic lineages). A library of insertional mutants for each HA was generated and deep sequenced after passaging to determine where insertions were tolerated in replicating viruses.

2018-06-05 | GSE113831 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data