Growth phase-dependent composition of the Helicobacter pylori exoproteome.

Snider CA, Voss BJ, McDonald WH, Cover TL
J Proteomics. 2016 130: 94-107

PMID: 26363098 · PMCID: PMC4640983 · DOI:10.1016/j.jprot.2015.08.025

Helicobacter pylori colonizes the human stomach and is associated with an increased risk of gastric cancer and peptic ulcer disease. Analysis of H. pylori protein secretion is complicated by the occurrence of bacterial autolysis. In this study, we analyzed the exoproteome of H. pylori at multiple phases of bacterial growth and identified 74 proteins that are selectively released into the extracellular space. These include proteins known to cause alterations in host cells, antigenic proteins, and additional proteins that have not yet been studied in any detail. The composition of the H. pylori exoproteome is dependent on the phase of bacterial growth. For example, the proportional abundance of the vacuolating toxin VacA in culture supernatant is higher during late growth phases than early growth phases, whereas the proportional abundance of many other proteins is higher during early growth phases. We detected marked variation in the subcellular localization of putative secreted proteins within soluble and membrane fractions derived from intact bacteria. By providing a comprehensive view of the H. pylori exoproteome, these results provide new insights into the array of secreted H. pylori proteins that may cause alterations in the gastric environment.

Published by Elsevier B.V.

MeSH Terms (13)

Bacterial Proteins Cluster Analysis Gastritis Gene Expression Regulation, Bacterial Helicobacter Infections Helicobacter pylori Humans Mass Spectrometry Protein Sorting Signals Proteome Proteomics Solubility Stomach

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