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Properties of the HtrA protease from bacterium Helicobacter pylori whose activity is indispensable for growth under stress conditions

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cris.lastimport.scopus2024-02-12T20:49:36Z
dc.abstract.enThe protease high temperature requirement A from the gastric pathogen Helicobacter pylori (HtrAHp) belongs to the well conserved family of serine proteases. HtrAHp 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 HtrAHp in the H. pylori cell physiology due to the lack of htrA knockout strains. Here, using a newly constructed 1htrA mutant strain, we found that bacteria deprived of HtrAHp 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 HtrAHp plays a protective role in the H. pylori cell, presumably associated with maintenance of important periplasmic and outer membrane proteins. Purified HtrAHp 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, HtrAHp showed the capability to regain its active structure following treatment under denaturing conditions. Taken together, our work demonstrates that HtrAHp 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.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorModrak-Wójcik, Anna
dc.contributor.authorLipińska, Barbara
dc.contributor.authorSkórko-Glonek, Joanna
dc.contributor.authorApanowicz, Małgorzata
dc.contributor.authorLesner, Adam
dc.contributor.authorFigaj, Donata
dc.contributor.authorPAWLIK, ANNA
dc.contributor.authorZarzecka, Urszula
dc.contributor.authorBzowska, Maria
dc.contributor.authorBacker, Steffen
dc.date.accessioned2024-01-25T18:13:35Z
dc.date.available2024-01-25T18:13:35Z
dc.date.copyright2019-05-03
dc.date.issued2019
dc.description.accesstimeAT_PUBLICATION
dc.description.financeNie dotyczy
dc.description.versionFINAL_PUBLISHED
dc.description.volume10
dc.identifier.doi10.3389/FMICB.2019.00961
dc.identifier.issn1664-302X
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/117249
dc.identifier.weblinkhttps://repozytorium.bg.ug.edu.pl/info/article/UOG84595ad1c6a24b6093809d1885919683/
dc.languageeng
dc.pbn.affiliationphysical sciences
dc.relation.ispartofFrontiers in Microbiology
dc.relation.pages1-16
dc.rightsCC-BY
dc.sciencecloudnosend
dc.subject.enHtrA
dc.subject.enHelicobacter pylori
dc.subject.envirulent factor
dc.subject.enproteolytic activity
dc.subject.enprotein quality control system
dc.subject.enstress endurance
dc.subject.enoligomerization
dc.titleProperties of the HtrA protease from bacterium Helicobacter pylori whose activity is indispensable for growth under stress conditions
dc.typeJournalArticle
dspace.entity.typePublication