Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition [I]

ABSTRACT: Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition [I]

PROVIDER: PRJNA744159 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR15049603_1.fastq.gz	Fastqsanger.gz
	SRR15049603_2.fastq.gz	Fastqsanger.gz
	SRR15049604_1.fastq.gz	Fastqsanger.gz
	SRR15049604_2.fastq.gz	Fastqsanger.gz
	SRR15049605_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 128

Similar Datasets

Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition [II]

Project description:The microbial cell surface is a critical site of microbe-host interactions that often control infection outcomes. Defining the set of host proteins present at this interface has been challenging. Here, we used a surface biotinylation approach coupled to quantitative mass spectrometry to identify and quantify both bacterial and host proteins present on the surface of diarrheal fluid-derived V. cholerae in an infant rabbit model of cholera. Our data showed that V. cholerae surfaces were coated with numerous host proteins, whose abundance were driven by the presence of cholera toxin, including the C type lectin SP-D. Mice lacking SP-D had enhanced V. cholerae intestinal colonization. Additional host proteins (AnxA1, LPO and ZAG) capable of binding V. cholerae were also found to recognize distinct taxa of the murine intestinal microbiota, suggesting that these host factors may play roles in intestinal homeostasis in addition to host defense. Proteomic analysis of microbial surfaces is valuable for identifying host interactions that regulate infection and homeostasis with both pathogens and endogenous microbiota alike.

2021-07-08 | GSE179529 | GEO

Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition [I]

2021-07-08 | GSE179528 | GEO

Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition

Project description:Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition

| PRJNA744149 | ENA

Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition [II]

Project description:Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition [II]

| PRJNA744163 | ENA

Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition

2021-10-02 | PXD027076 | Pride

Proteomic analysis of the pathogen surface in cholera identifies host proteins involved in defense and microbiota recognition

Project description:This SuperSeries is composed of the SubSeries listed below.

2021-07-08 | GSE179530 | GEO

Chemoproteomic profiling of host and pathogen enzymes active in cholera

Project description:Activity-based protein profiling (ABPP) is a chemoproteomic tool for detecting active enzymes in complex biological systems. We used ABPP to identify secreted bacterial and host serine hydrolases that are active in animals infected with the cholera pathogen Vibrio cholerae. Four V. cholerae proteases were consistently active in infected rabbits, and one, VC0157 (renamed IvaP), was also active in human cholera stool. Inactivation of IvaP influenced the activity of other secreted V. cholerae and rabbit enzymes in vivo, while genetic disruption of all four proteases increased the abundance and binding of an intestinal lectin—intelectin—to V. cholerae in infected rabbits. Intelectin also bound to other enteric bacterial pathogens, suggesting it may constitute a previously unrecognized mechanism of bacterial surveillance in the intestine that is inhibited by pathogen-secreted proteases. Our work demonstrates the power of activity-based proteomics to reveal host-pathogen enzymatic dialogue in an animal model of infection.

2016-02-22 | PXD003000 | Pride

Vibrio Cholera from Bangladesh

Project description:Vibrio Cholera from Bangladesh

| PRJEB18714 | ENA

Genome-wide effect of cholera toxin and nitrate treatment in etiolated rice plants

Project description:The present study used microarray approach to identify the genomewide response to cholera toxin in the presence of nitrate. Considering that fact that the possibility of the existence of multiple Gα genes/proteins in plants has not been conclusively ruled out, analysis of the genomewide impact of RGA1 mutation in rice and GPA1 mutation in Arabidopsis reveal only those genes that are under their direct control. On the other hand, assuming that all those different Gα subunits in any given plant are regulated by cholera toxin, analysis of the genomwide response to cholera toxin could capture the entire G-protein responsive transcriptome, beyond what can be revealed by the mutant approach. This could reveal even those genes that respond to other, as yet unidentified Gα subunits, as well as reveal some genes that are non-specifically regulated by cholera toxin, independent of any G-proteins.

2010-12-01 | GSE20924 | GEO

Hainan cholera outbreak

Project description:Genomic analysis of Hainan cholera outbreak

| PRJEB8241 | ENA