SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens
In the Gram-negative bacteria, many important virulence factors reach their destination via two-step export systems, and they must traverse the periplasmic space before reaching the outer membrane. Since these proteins must be maintained in a structure competent for transport into or across the memb...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/1/295 |
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| author | Donata Figaj Patrycja Ambroziak Iga Rzepka Joanna Skórko-Glonek |
| author_facet | Donata Figaj Patrycja Ambroziak Iga Rzepka Joanna Skórko-Glonek |
| author_sort | Donata Figaj |
| collection | DOAJ |
| description | In the Gram-negative bacteria, many important virulence factors reach their destination via two-step export systems, and they must traverse the periplasmic space before reaching the outer membrane. Since these proteins must be maintained in a structure competent for transport into or across the membrane, they frequently require the assistance of chaperones. Based on the results obtained for the model bacterium <i>Escherichia coli</i> and related species, it is assumed that in the biogenesis of the outer membrane proteins and the periplasmic transit of secretory proteins, the SurA peptidyl–prolyl isomerase/chaperone plays a leading role, while the Skp chaperone is rather of secondary importance. However, detailed studies carried out on several other Gram-negative pathogens indicate that the importance of individual chaperones in the folding and transport processes depends on the properties of client proteins and is species-specific. Taking into account the importance of SurA functions in bacterial virulence and severity of phenotypes due to <i>surA</i> mutations, this folding factor is considered as a putative therapeutic target to combat microbial infections. In this review, we present recent findings regarding SurA and Skp proteins: their mechanisms of action, involvement in processes related to virulence, and perspectives to use them as therapeutic targets. |
| first_indexed | 2024-03-11T09:59:58Z |
| format | Article |
| id | doaj.art-926fbf24eb3443d6980fba79ee7fa5f1 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T09:59:58Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-926fbf24eb3443d6980fba79ee7fa5f12023-11-16T15:31:17ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-12-0124129510.3390/ijms24010295SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial PathogensDonata Figaj0Patrycja Ambroziak1Iga Rzepka2Joanna Skórko-Glonek3Department of General and Medical Biochemistry, Faculty of Biology, University of Gdansk, Wita Stwosza 59, 80-308 Gdansk, PolandDepartment of General and Medical Biochemistry, Faculty of Biology, University of Gdansk, Wita Stwosza 59, 80-308 Gdansk, PolandDepartment of General and Medical Biochemistry, Faculty of Biology, University of Gdansk, Wita Stwosza 59, 80-308 Gdansk, PolandDepartment of General and Medical Biochemistry, Faculty of Biology, University of Gdansk, Wita Stwosza 59, 80-308 Gdansk, PolandIn the Gram-negative bacteria, many important virulence factors reach their destination via two-step export systems, and they must traverse the periplasmic space before reaching the outer membrane. Since these proteins must be maintained in a structure competent for transport into or across the membrane, they frequently require the assistance of chaperones. Based on the results obtained for the model bacterium <i>Escherichia coli</i> and related species, it is assumed that in the biogenesis of the outer membrane proteins and the periplasmic transit of secretory proteins, the SurA peptidyl–prolyl isomerase/chaperone plays a leading role, while the Skp chaperone is rather of secondary importance. However, detailed studies carried out on several other Gram-negative pathogens indicate that the importance of individual chaperones in the folding and transport processes depends on the properties of client proteins and is species-specific. Taking into account the importance of SurA functions in bacterial virulence and severity of phenotypes due to <i>surA</i> mutations, this folding factor is considered as a putative therapeutic target to combat microbial infections. In this review, we present recent findings regarding SurA and Skp proteins: their mechanisms of action, involvement in processes related to virulence, and perspectives to use them as therapeutic targets.https://www.mdpi.com/1422-0067/24/1/295SurASkpperiplasmic folding factorsvirulence factorsprotein foldingPQCS |
| spellingShingle | Donata Figaj Patrycja Ambroziak Iga Rzepka Joanna Skórko-Glonek SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens International Journal of Molecular Sciences SurA Skp periplasmic folding factors virulence factors protein folding PQCS |
| title | SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens |
| title_full | SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens |
| title_fullStr | SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens |
| title_full_unstemmed | SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens |
| title_short | SurA-like and Skp-like Proteins as Important Virulence Determinants of the Gram Negative Bacterial Pathogens |
| title_sort | sura like and skp like proteins as important virulence determinants of the gram negative bacterial pathogens |
| topic | SurA Skp periplasmic folding factors virulence factors protein folding PQCS |
| url | https://www.mdpi.com/1422-0067/24/1/295 |
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