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Bacterial Proteases in Helicobacter pylori Infections and Gastric Disease

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Helicobacter pylori and Gastric Cancer

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 444))

Abstract

Helicobacter pylori (H. pylori) proteases have become a major focus of research in recent years, because they not only have an important function in bacterial physiology, but also directly alter host cell functions. In this review, we summarize recent findings on extracellular H. pylori proteases that target host-derived substrates to facilitate bacterial pathogenesis. In particular, the secreted H. pylori collagenase (Hp0169), the metalloprotease Hp1012, or the serine protease High temperature requirement A (HtrA) are of great interest. Specifically, various host cell-derived substrates were identified for HtrA that directly interfere with the gastric epithelial barrier allowing full pathogenesis. In light of increasing antibiotic resistance, the development of inhibitory compounds for extracellular proteases as potential targets is an innovative field that offers alternatives to existing therapies.

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Acknowledgements

The work of SW was supported by the grant I_4360 and P_31507 from the Austrian Science Fund (FWF).

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Authors and Affiliations

  1. Department of Biosciences and Medical Biology, Laboratory for Microbial Infection and Cancer, Paris-Lodron University of Salzburg, Salzburg, Austria

    Silja Wessler & Gernot Posselt

  2. Cancer Cluster Salzburg and Allergy-Cancer-BioNano Research Centre, Salzburg, Austria

    Silja Wessler & Gernot Posselt

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  1. Silja Wessler
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  2. Gernot Posselt
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Correspondence to Silja Wessler .

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  1. Department of Biology, Division of Microbiology, University of Erlangen-Nuremberg, Erlangen, Bayern, Germany

    Steffen Backert

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Wessler, S., Posselt, G. (2023). Bacterial Proteases in Helicobacter pylori Infections and Gastric Disease. In: Backert, S. (eds) Helicobacter pylori and Gastric Cancer. Current Topics in Microbiology and Immunology, vol 444. Springer, Cham. https://doi.org/10.1007/978-3-031-47331-9_10

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