Dataset Information

Comparison of culture supernatants from wild-type Vibrio cholerae and a mutant lacking the PDZ domain of the type II secretion system

ABSTRACT: The culture supernatant of wild-type (WT) Vibrio cholerae N16961 and mutant epsC∆PDZ strains were compared to determine which, if any, type II secretion system substrates were affected by the deletion of the PDZ domain of EpsC

INSTRUMENT(S):

ORGANISM(S): Vibrio Cholerae Serotype O1 (strain Atcc 39315 / El Tor Inaba N16961)

SUBMITTER: Maria Sandkvist

LAB HEAD: Maria Sandkvist, PhD

PROVIDER: PXD062995 | Pride | 2025-08-25

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	MSB51240Band_01.raw	Raw
	MSB51240Band_01__F171718_.mzid	Mzid
	MSB51240Band_01__F171718_.mzid_MSB51240Band_01__F171718_.MGF	Mzid
	MSB51240Band_02.raw	Raw
	MSB51240Band_02__F171719_.mzid	Mzid

Items per page:

1 - 5 of 180

Publications

The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system in Vibrio cholerae.

Shannon Austin A Johnson Tanya T Roberts Cameron S CS Chaton Catherine T CT Korotkov Konstantin V KV Sandkvist Maria M

Journal of bacteriology 20250714 8

The Type II Secretion System (T2SS) of the Gram-negative pathogen Vibrio cholerae is considered a virulence factor primarily because it facilitates the secretion of cholera toxin upon arrival of this pathogen in the human intestinal lumen, resulting in the profuse watery diarrhea associated with infection. Results from transposon mutagenesis screens suggest that the V. cholerae eps genes that code for the T2SS are essential. The deletion of these genes impairs the secretion of the ...[more]

PMID: 40657929

Similar Datasets

Project description:Tumor cells are known to induce tumor-supporting phenotypes in surrounding stroma cells which leads to the creation of a favourable tumor niche and sustained growth as well as progression of the tumor. One mechanism how tumor cells can modulate surrounding stroma cells is through the release of extracellular vesicles. These vesicles comprise large plasma membrane-derived microvesicles (diameter 100-1000 nm) as well as the better characterized smaller exosomes (diameter <100 nm) which are derived from intraluminal vesicles inside endosomal compartments. In spite of the identification of vesicle-mediated tumor-tumor and tumor-stroma intracellular communication loops, the tumor-supporting factors present on tumor vesicles as well as the factors that regulate their export are largely unknown. One attractive candidate protein which could be involved in controlling vesicular cargo selection is the adaptor scaffolding protein syntenin/SDCBP, which is known as a marker protein highly expressed on exosomes. Syntenin is characterized by two structural protein interaction modules, the PDZ domains, which can either bind to other PDZ domains or to the C-terminus of target proteins in a sequence-specific way, thereby enabling protein-protein interactions. PDZ proteins in general are known to be involved in the recruitment and assembly of specific protein complexes, especially at the cellular plasma membrane. Syntenin is a factor that has been shown to control not only the biogenesis of exosomes, but also the sorting of specific proteins to these vesicles. While it is highly expressed in human fetal tissues, its expression is significantly downregulated in adult tissues with the exception of the heart or placenta. However, high levels of syntenin seem to be restored in advanced human cancer of different entities and thereby suggest a role for syntenin in tumor progression. Previous results from the group of Pascale Zimmermann showed that syntenin is of particular importance for regulating the sorting of its (known) target proteins to exosomes which would allow their distribution to neighboring stroma cells. To analyze which tumor-supporting factors are present on breast cancer exosomes and which of them are regulated by syntenin, exosomes from 4T1 wildtype cells (syntenin-high) and from two clones of syntenin CRISPR/Cas9 syntenin knockout cells were isolated from cell culture supernatants by differential ultracentrifugation and then analyzed and compared by label-free mass spectrometry.

Project description:T lymphocyte recognition of antigenic peptides on the surface of antigen-presenting cells (APC) leads to immune synapse formation (IS). By analogy with the nervous synapse, this cell-cell communication model requires the formation of highly organized structures that delimit an active zone of membrane traffic. For T cells to connect antigen recognition with the biological response, receptors and signaling proteins must be recycled. Sorting nexin 27 (SNX27) is an endosomal protein best known for its role in recycling PDZ (PSD95, Dlg1, ZO-1)-interacting neuronal proteins via the retromer transport machinery. Alteration of this sorting pathway leads to neurodegeneration and is associated to Down syndrome, Alzheimer’s and Parkinson’s diseases. In T lymphocytes, SNX27 interacts with diacylglycerol kinase zeta (DGKz), which provides a mechanistic link between diacylglycerol metabolism and membrane trafficking. Following antigen recognition, SNX27-positive endosomes polarize to the IS and a PDZ-dependent SNX27 pool accumulates at the cell-cell contact area. To test for additional SNX27 functions, we carried out proteomic analysis of the SNX27 interactome purified from T cells in contact with APC, and identified SNX27 interaction with the retromer and with members of the WASH (Wiskott-Aldrich syndrome protein and SCAR homologue) complex. This finding indicates the conserved nature of the SNX27/WASH/retromer complex in hematopoietic cells and suggests similarity between neurological diseases and abnormal immune/inflammatory responses. We also found PDZ-dependent SNX27 cargoes, including modulators of cytoskeletal reorganization such as zona occludens-2 (ZO-2). ZO-2, a cytosolic component of epithelial cell-cell junctions, localized to the IS, and SNX27 silencing affected ZO-2 stability at the synapse. This study broadens our knowledge of SNX27 function in T lymphocytes, and suggests that pathways that delimit polarized structures in epithelial systems also participate in IS regulation.

Dataset Information

Comparison of culture supernatants from wild-type Vibrio cholerae and a mutant lacking the PDZ domain of the type II secretion system

Dataset's files

Publications

The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system in <i>Vibrio cholerae</i>.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Dataset Information

Comparison of culture supernatants from wild-type Vibrio cholerae and a mutant lacking the PDZ domain of the type II secretion system

Dataset's files

Publications

The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system in &lt;i&gt;Vibrio cholerae&lt;/i&gt;.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system in <i>Vibrio cholerae</i>.