Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

PROVIDER: PRJNA801090 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR17831836_1.fastq.gz	Fastqsanger.gz
	SRR17831836_2.fastq.gz	Fastqsanger.gz
	SRR17831837_1.fastq.gz	Fastqsanger.gz
	SRR17831837_2.fastq.gz	Fastqsanger.gz

Items per page:

1 - 4 of 4

Similar Datasets

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

Deep mutational scan of a drug efflux pump reveals its structure-function landscape

Project description:Drug efflux is a common resistance mechanism found in bacteria and cancer cells. Although several structures of drug efflux pumps are available, they provide only limited functional information on the phenomenon of drug efflux. Here, we performed deep mutational scanning (DMS) on the bacterial ATP binding cassette (ABC) transporter EfrCD from Enterococcus faecalis to determine the drug efflux activity profile of more than 1400 single variants

2021-11-25 | GSE189399 | GEO

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

| PRJNA1083715 | ENA

Project description:Deep mutational scanning of avian influenza PB2 to identify pimodivir resistance mutations

| PRJNA719471 | ENA

Project description:SHP2 deep mutational scanning

| PRJNA1232161 | 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

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

Project description:Rad54 deep mutational scanning data

| PRJNA1235687 | ENA

Project description:Deep mutational scanning of hOCT1

| PRJNA980726 | ENA