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Characterization of the Na+-NQR from V. cholerae

ABSTRACT: The Na+-pumping NADH-ubiquinone oxidoreductase (Na+-NQR) is anticipated to be a promising target of antibiotics because it is an exclusively prokaryotic enzyme and plays an essential role in bioenergetics in many pathogenic bacteria. To identify the site labeled by a ubiquinone probe, the NqrA subunit was partially digested with V8-protease. The partial digests were subjected to "in-gel" tryptic digestion, followed by MALDI-TOF MS analysis.

ORGANISM(S): Vibrio Cholerae

SUBMITTER: Hideto Miyoshi

PROVIDER: PXD029801 | JPOST Repository | Sat Nov 19 00:00:00 GMT 2022

REPOSITORIES: jPOST

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Project description:Background: Acute respiratory distress syndrome (ARDS) is characterized by refractory hypoxemia caused by accumulation of pulmonary fluid, which is related to inflammatory cell infiltration, impaired tight junction of pulmonary epithelium and impaired Na, K-ATPase function, especially Na, K-ATPase α1 subunit. Up until now, the pathogenic mechanism at the level of protein during lipopolysaccharide- (LPS-) induced ARDS remains unclear. Methods: Using an unbiased, discovery and quantitative proteomic approach, we discovered the differentially expressed proteins binding to Na, K-ATPase α1 between LPS-A549 cells and Control-A549 cells. These Na, K-ATPase α1 interacting proteins were screened by co-immunoprecipitation (Co-IP) technology. Among them, some of the differentially expressed proteins with significant performance were identified and quantified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). The protein interaction network was constructed by the related Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis. Several differentially expressed proteins were validated by Western blot. Results: Of identified 1598 proteins, 89 were differentially expressed proteins between LPS-A549 cells and Control-A549 cells. Intriguingly, protein-protein interaction network showed that there were 244 significantly enriched co-expression among 60 proteins in the group control-A549. while the group LPS-A549 showed 43 significant enriched interactions among 29 proteins. The related GO and KEGG analysis found evident phenomena of ubiquitination and deubiquitination, as well as the pathways related to autophagy. Among proteins with rich abundance, there were several intriguing ones, including the deubiquitinase (OTUB1), the tight junction protein zonula occludens-1 (ZO-1), the scaffold protein in CUL4B-RING ubiquitin ligase (CRL4B) complexes (CUL4B) and the autophagy-related protein sequestosome-1 (SQSTM1). Conclusions: In conclusion, our proteomic approach revealed targets related to the occurrence and development of ARDS, being the first study to investigate significant differences in Na, K-ATPase α1 interacting proteins between LPS-induced ARDS cell model and control-A549 cell. These proteins may help the clinical diagnosis and facilitate the personalized treatment of ARDS.

			Action	DRS
	1507_MSMS_Spectrum.mzXML	Mzxml
	2058_MSMS_Spectrum.mzXML	Mzxml
	A1_Spectrum.mzXML	Mzxml
	A2_Spectrum.mzXML	Mzxml
	A3_Spectrum.mzXML	Mzxml

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Characterization of the Na+-NQR from V. cholerae

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