Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Overexpressing the ClpC AAA+ Unfoldase Prematurely Triggers Secondary Differentiation in Chlamydia trachomatis

ABSTRACT: Overexpressing the ClpC AAA+ Unfoldase Prematurely Triggers Secondary Differentiation in Chlamydia trachomatis

PROVIDER: PRJNA1075127 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR27931661_1.fastq.gz	Fastqsanger.gz
	SRR27931661_2.fastq.gz	Fastqsanger.gz
	SRR27931662_1.fastq.gz	Fastqsanger.gz
	SRR27931662_2.fastq.gz	Fastqsanger.gz
	SRR27931663_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 24

Similar Datasets

Overexpressing the ClpC AAA+ Unfoldase Prematurely Triggers Secondary Differentiation in Chlamydia trachomatis

Project description:Chlamydia is an obligate intracellular bacteria that undergoes a complex biphasic developmental cycle, alternating between the smaller infectious non-dividing elementary body (EB) and the larger non-infectious but dividing reticulate body (RB). Due to the differences between these functionally and morphologically distinct forms, we hypothesize protein degradation is essential to chlamydial differentiation. The bacterial Clp system, consisting of an ATPase unfoldase (e.g., ClpX or ClpC) and a proteolytic component (e.g., ClpP), is critical for the physiology of bacteria through its recognition, and usually degradation, of specific substrates. We observed by transmission electron microscopy that overexpression of wild-type ClpC, but not an ATPase mutant isoform, in Chlamydia increased glycogen accumulation within the vacuolar niche of the bacteria earlier in the developmental cycle than typically observed. This suggested ClpC activity may increase expression of EB-associated genes. Consistent with this, targeted RT-qPCR analyses demonstrated a significant increase in several EB-associated gene transcripts earlier in development. These effects were not observed with overexpression of the ATPase mutant of ClpC, providing strong evidence that the activity of ClpC drives secondary differentiation. By analyzing the global transcriptional response to ClpC overexpression using RNA sequencing, we observed a global shift to earlier expression of canonical late developmental cycle genes and other EB-associated genes. Finally, we directly linked overexpression of ClpC with earlier production of EBs. Conversely, disrupting normal ClpC function with an ATPase mutant caused a delay in secondary differentiation. Overall, these findings provide the first mechanistic insight for initiation of secondary differentiation in Chlamydia.

2024-11-12 | GSE255503 | GEO

Heat shock-induced transcriptomic response in Chlamydia trachomatis

Project description:Heat shock-induced transcriptomic response in Chlamydia trachomatis

2021-12-08 | GSE173366 | GEO

Progesterone activates multiple innate immune pathways in Chlamydia trachomatis-infected endocervical cells

Project description:In this project we examined the in-vitro effect of female sex hormones (estradiol and progesterone at average physiological concentrations) during a infection mediated by Chlamydia trachomatis serovar D, on the gene expression of human endometrial cell line ECC-1 The effects of the female sex hormones progesterone and oestradiol while infected by Chlamydia trachomatis were examined at two timepoints.

2011-08-02 | E-GEOD-31149 | biostudies-arrayexpress

C. trachomatis L2 inclusion proteome

Project description:Chlamydia trachomatis is an important human pathogen that replicates inside the infected host cell in a unique vacuole, the inclusion. The formation of this intracellular bacterial niche is essential for productive Chlamydia infections. Despite its importance for Chlamydia biology, a holistic view on the protein composition of the inclusion, including its membrane, is currently missing. Here we describe a newly established method to purify inclusions from C. trachomatis infected epithelial cells and the analysis of the host cell-derived proteome by a combination of label free and stable isotope labeling -based quantitative proteomics. Computational analysis of the proteome data indicated that the inclusion is a complex intracellular trafficking platform that interacts with host cells' antero- and retrograde trafficking pathways. Furthermore, the inclusion is highly enriched for sorting nexins of the SNX-BAR retromer, a complex essential for retrograde trafficking. Functional studies showed that in particular SNX5 controls the C. trachomatis infection and that retrograde trafficking is essential for infectious progeny formation. In summary, our findings suggest that the inclusion of C. trachomatis is well embedded in the hosts' endomembrane system and hijacks retrograde trafficking pathways for effective infection.

2015-06-08 | PXD002113 | Pride

Indoleamine 2,3-dioxygenase cannot inhibit Chlamydia trachomatis growth in HL-60 human neutrophil granulocytes

Project description:Neutrophil granulocytes are the major cells involved in the Chlamydia trachomatis (C.trachomatis)-mediated inflammation and histopathology. A key gene in human intracellular antichlamydial defense is the tryptophan degrading enzyme indoleamine 2,3-dioxygenase (IDO), which limits the growth of the tryptophan auxotroph Chlamydia. Despite its importance, the role of IDO in the intracellular defense against Chlamydia in neutrophils has not yet been characterized. Affymetrix microarrays were used to obtain global gene expression data for monitoring the effect of C. trachomatis serovar D infection on the transcriptome of human neutrophil granulocytes.

2021-11-08 | GSE180238 | GEO

Quantitative phospho-proteomic analysis of human endocervical epithelial cells infected with Chlamydia trachomatis

Project description:Human A2EN endocervical epithelial cells infected with Chlamydia trachomatis

2022-11-03 | MSV000090636 | MassIVE

Expression data of A2EN cells during early stage of Chlamydia trachomatis infection

Project description:Chlamydia trachomatis is an obligate intracellular pathogen that causes trachoma and sextually transmitted disease in human. During early stage of infection, Chlamydia secreted bacterial effector proteins into host cell cytoplasm to help its entry and estabilishment of early replicated niche. We identified a Chlamydia mutant that lack an early Effector. To address the function of this effector, we infected A2EN cells with this mutant (G1V) and its complemented counterpart (G1TEPP) to see what host gene transcriptions are affected by this effector. A2EN cells were mock infected, or infected with a Chlamydia mutant or its complemented counterpart for 4 hour post infection.

2014-04-09 | E-GEOD-54336 | biostudies-arrayexpress

RNA Seq analysis of Chlamydia trachomatis D serovar in axenic culture

Project description:Chlamydia trachomatis D serovar was grown in axenic culture with G6P or G6P with glutamine. The data reveal the early transcriptonal regulation in the bacteria.

2020-07-16 | GSE147539 | GEO

Transcriptome profiling of endometrial biopsies inflammatory response to Chlamydia trachomatis genital tract infection

Project description:Chlamydia trachomatis is an obligate intracellular Gram-negative bacterium that frequently causes an asymptomatic genital tract infection, gradually cleared by host immunity Transcriptome profiles were made of endometrial tissue from women with or without genital tract C. trachomatis infection, to characterize host responses to infection. Profiles showed that infection polarized host defense toward Type 2 immune responses. Responses included fibrin deposition, enhanced wound repair, and tissue remodeling. Trans-cervical endometrial biopsy specimens were collected from 10 women with no identified upper or lower genital tract infection and 12 women with C. trachomatis endometrial infection.

2013-03-01 | E-GEOD-41075 | biostudies-arrayexpress

Proximity-dependent proteomics of the Chlamydia trachomatis inclusion membrane (revised)

Project description:Proximity-dependent proteomics of the Chlamydia trachomatis inclusion membrane reveals functional interactions with endoplasmic reticulum exit sites.

2019-08-27 | PXD012494 | Pride

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