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Properties of the HtrA Protease From Bacterium Helicobacter pylori Whose Activity Is Indispensable for Growth Under Stress Conditions
The protease high temperature requirement A from the gastric pathogen (HtrA ) belongs to the well conserved family of serine proteases. HtrA is an important secreted virulence factor involved in the disruption of tight and adherens junctions during infection. Very little is known about the function...
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Published in: | Frontiers in microbiology 2019-05, Vol.10, p.961-961 |
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Main Authors: | , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The protease high temperature requirement A from the gastric pathogen
(HtrA
) belongs to the well conserved family of serine proteases. HtrA
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
in the
cell physiology due to the lack of
knockout strains. Here, using a newly constructed Δ
mutant strain, we found that bacteria deprived of HtrA
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
plays a protective role in the
cell, presumably associated with maintenance of important periplasmic and outer membrane proteins. Purified HtrA
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 (T
) values of above 85°C. Moreover, HtrA
showed the capability to regain its active structure following treatment under denaturing conditions. Taken together, our work demonstrates that HtrA
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. |
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ISSN: | 1664-302X 1664-302X |
DOI: | 10.3389/fmicb.2019.00961 |