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Moonlighting of Helicobacter pylori catalase protects against complement-mediated killing by utilising the host molecule vitronectin

Richter, Corinna LU ; Mukherjee, Oindrilla LU ; Ermert, David LU ; Singh, Birendra LU ; Su, Yu Ching LU ; Agarwal, Vaibhav LU ; Blom, Anna M. LU orcid and Riesbeck, Kristian LU orcid (2016) In Scientific Reports 6.
Abstract

Helicobacter pylori is an important human pathogen and a common cause of peptic ulcers and gastric cancer. Despite H. pylori provoking strong innate and adaptive immune responses, the bacterium is able to successfully establish long-term infections. Vitronectin (Vn), a component of both the extracellular matrix and plasma, is involved in many physiological processes, including regulation of the complement system. The aim of this study was to define a receptor in H. pylori that binds Vn and determine the significance of the interaction for virulence. Surprisingly, by using proteomics, we found that the hydrogen peroxide-neutralizing enzyme catalase KatA is a major Vn-binding protein. Deletion of the katA gene in three different strains... (More)

Helicobacter pylori is an important human pathogen and a common cause of peptic ulcers and gastric cancer. Despite H. pylori provoking strong innate and adaptive immune responses, the bacterium is able to successfully establish long-term infections. Vitronectin (Vn), a component of both the extracellular matrix and plasma, is involved in many physiological processes, including regulation of the complement system. The aim of this study was to define a receptor in H. pylori that binds Vn and determine the significance of the interaction for virulence. Surprisingly, by using proteomics, we found that the hydrogen peroxide-neutralizing enzyme catalase KatA is a major Vn-binding protein. Deletion of the katA gene in three different strains resulted in impaired binding of Vn. Recombinant KatA was generated and shown to bind with high affinity to a region between heparin-binding domain 2 and 3 of Vn that differs from previously characterised bacterial binding sites on the molecule. In terms of function, KatA protected H. pylori from complement-mediated killing in a Vn-dependent manner. Taken together, the virulence factor KatA is a Vn-binding protein that moonlights on the surface of H. pylori to promote bacterial evasion of host innate immunity.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scientific Reports
volume
6
article number
24391
publisher
Nature Publishing Group
external identifiers
  • pmid:27087644
  • wos:000374227800001
  • scopus:84973127098
ISSN
2045-2322
DOI
10.1038/srep24391
language
English
LU publication?
yes
id
7ad5f90a-94c1-4c5e-b086-8e73a88d96b6
date added to LUP
2016-06-30 13:22:20
date last changed
2024-03-07 09:04:14
@article{7ad5f90a-94c1-4c5e-b086-8e73a88d96b6,
  abstract     = {{<p>Helicobacter pylori is an important human pathogen and a common cause of peptic ulcers and gastric cancer. Despite H. pylori provoking strong innate and adaptive immune responses, the bacterium is able to successfully establish long-term infections. Vitronectin (Vn), a component of both the extracellular matrix and plasma, is involved in many physiological processes, including regulation of the complement system. The aim of this study was to define a receptor in H. pylori that binds Vn and determine the significance of the interaction for virulence. Surprisingly, by using proteomics, we found that the hydrogen peroxide-neutralizing enzyme catalase KatA is a major Vn-binding protein. Deletion of the katA gene in three different strains resulted in impaired binding of Vn. Recombinant KatA was generated and shown to bind with high affinity to a region between heparin-binding domain 2 and 3 of Vn that differs from previously characterised bacterial binding sites on the molecule. In terms of function, KatA protected H. pylori from complement-mediated killing in a Vn-dependent manner. Taken together, the virulence factor KatA is a Vn-binding protein that moonlights on the surface of H. pylori to promote bacterial evasion of host innate immunity.</p>}},
  author       = {{Richter, Corinna and Mukherjee, Oindrilla and Ermert, David and Singh, Birendra and Su, Yu Ching and Agarwal, Vaibhav and Blom, Anna M. and Riesbeck, Kristian}},
  issn         = {{2045-2322}},
  language     = {{eng}},
  month        = {{04}},
  publisher    = {{Nature Publishing Group}},
  series       = {{Scientific Reports}},
  title        = {{Moonlighting of Helicobacter pylori catalase protects against complement-mediated killing by utilising the host molecule vitronectin}},
  url          = {{http://dx.doi.org/10.1038/srep24391}},
  doi          = {{10.1038/srep24391}},
  volume       = {{6}},
  year         = {{2016}},
}