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- Title
Properties of the HtrA Protease From Bacterium Helicobacter pylori Whose Activity Is Indispensable for Growth Under Stress Conditions.
- Authors
Zarzecka, Urszula; Modrak-Wójcik, Anna; Figaj, Donata; Apanowicz, Malgorzata; Lesner, Adam; Bzowska, Agnieszka; Lipinska, Barbara; Zawilak-Pawlik, Anna; Backert, Steffen; Skorko-Glonek, Joanna
- Abstract
The protease high temperature requirement A from the gastric pathogen Helicobacter pylori (HtrA Hp) belongs to the well conserved family of serine proteases. HtrA Hp is an important secreted virulence factor involved in the disruption of tight and adherens junctions during infection. Very little is known about the function of HtrA Hp in the H. pylori cell physiology due to the lack of htrA knockout strains. Here, using a newly constructed Δ htrA mutant strain, we found that bacteria deprived of HtrA Hp showed increased sensitivity to certain types of stress, including elevated temperature, pH and osmotic shock, as well as treatment with puromycin. These data indicate that HtrA Hp plays a protective role in the H. pylori cell, presumably associated with maintenance of important periplasmic and outer membrane proteins. Purified HtrA Hp was shown to be very tolerant to a wide range of temperature and pH values. Remarkably, the protein exhibited a very high thermal stability with the melting point (Tm) values of above 85°C. Moreover, HtrA Hp showed the capability to regain its active structure following treatment under denaturing conditions. Taken together, our work demonstrates that HtrA Hp is well adapted to operate under harsh conditions as an exported virulence factor, but also inside the bacterial cell as an important component of the protein quality control system in the stressed cellular envelope.
- Subjects
HELICOBACTER pylori; HAPTOGLOBINS; SERINE proteinases; MEMBRANE proteins; ADHERENS junctions; CELL physiology
- Publication
Frontiers in Microbiology, 2019, pN.PAG
- ISSN
1664-302X
- Publication type
Article
- DOI
10.3389/fmicb.2019.00961