PXD050334

PXD050334 is an original dataset announced via ProteomeXchange.

Title	Helicobacter pylori gamma-glutamyltransferase relates to proteomic adaptations important for colonization
Description	Helicobacter pylori γ-glutamyltransferase (gGT) is a conserved virulence factor promoting bacterial colonization and immune tolerance. Although some studies addressed potential mechanisms explaining its function, the supportive role of gGT for in-vivo colonization remains unclear. In addition, it is unknown how differences in gGT expression observed for different strains may lead to compensatory mechanisms to ensure infection and persistence. Hence, it is of high importance to understand more profoundly the in-vivo function of this enzyme. In this study, we assessed acid survival under physiologic conditions mimicking the human gastric fluid and elevated the pH in the murine stomach prior to H. pylori infection to link gGT-mediated acid resistance to colonization. Furthermore, by comparing protein expression levels between wildtype and gGT-deficient H. pylori isolates before and after infecting mice, we systematically investigated proteomic adaptations of gGT-deficient bacteria during infection. Our data indicate that gGT plays a crucial role in sustaining urease activity in acidic environments, thereby supporting bacterial survival and successful colonization. The absence of gGT triggers the expression of proteins involved in nitrogen and iron metabolism, indicating a potential functional role of gGT in these metabolic pathways. Moreover, we observed an impaired growth of gGT-deficient strains in iron-restricted medium. In addition, the absence of gGT during infection leads to a significant overexpression of H. pylori adhesins and flagellar proteins, resulting in increased motility and adhesion capacity. In summary, we identified gGT-dependent mechanisms conferring a growth advantage to the bacterium in the gastric environment, which renders gGT a valuable target for the development of new treatments against H. pylori infection.
HostingRepository	PRIDE
AnnounceDate	2025-04-08
AnnouncementXML	Submission_2025-04-08_05:05:23.631.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nina Bach
SpeciesList	scientific name: Helicobacter pylori G27; NCBI TaxID: 563041; scientific name: Helicobacter pylori PMSS1; NCBI TaxID: 1431450;
ModificationList	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2024-03-04 12:18:51	ID requested
⏵ 1	2025-04-08 05:05:24	announced

Dataset with its publication pending

submitter keyword: in-vivo mouse infection, full proteome,Helicobacter pylori, secretome, LC-MS/MS

Stephan Axel Sieber
contact affiliation	Technical University of Munich (TUM), TUM School of Natural Sciences, Department Biosciences, Chair of Organic Chemistry II, Center for Functional Protein Assemblies (CPA), Ernst-Otto-Fischer Str. 8, Garching 85748, Germany
contact email	stephan.sieber@tum.de
lab head
Nina Bach
contact affiliation	TU München
contact email	nina.bach@tum.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD050334
     1. Label: PRIDE project
     2. Name: Helicobacter pylori gamma-glutamyltransferase relates to proteomic adaptations important for colonization