Invasion of Serratia proteamaculans is regulated by the sprI gene encoding AHL synthase

Tsaplina, Olga; Khmel, I. A.; Zaitseva, Yulia; Khaitlina, Sofia

doi:10.1016/j.micinf.2021.104852

Cited by 4 publications

(22 citation statements)

References 27 publications

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“…Our results show that, in contrast to the inactivation of the AHL synthase sprI gene [6], inactivation of the regulatory receptor protein sprR gene does not lead to an increase in the expression of the surface protein OmpX, which is responsible for adhesion, and does not affect the activity of protease protealysin, the substrate of which is OmpX. Despite the absence of an effect on adhesion, inactivation of the sprR gene leads to an increase in the invasive activity of S. proteamaculans correlated with the increase in the activity of extracellular metalloprotease serralysin, which is cytotoxic to mammalian cells.…”

Section: Introductioncontrasting

confidence: 57%

Section: Introductionsupporting

confidence: 51%

“…Previously we have shown that inactivation of the AHL synthase sprI gene resulted in a more than fourfold increase in the invasive activity of S. proteamaculans, preceded by the increase in bacterial adhesion to the cell surface [6]. To evaluate the contribution of another QS system component, regulatory receptor protein SprR, to the regulation of invasive activity of S. proteamaculans 94, we used a S. proteamaculans SprR(-) mutant carrying the inactivated receptor sprR gene.…”

Section: The Effects Of the Receptor Sprr Gene Inactivation On The S Proteamaculans Invasive Activitymentioning

confidence: 99%

“…Previously, we have shown that inactivation of the AHL synthase sprI gene resulted in the increase in invasive activity of S. proteamaculans preceded by the increased bacterial adhesion to the cell surface [6]. By our data, the increased adhesion of S. proteamaculans SprI(-) could be caused by both an increase in the expression of the surface protein OmpX responsible for adhesion [6][7][8] and a decrease in the activity of protease protealysin, whose substrate is OmpX [7,8]. On the other hand, the AHL signaling molecules can directly affect host cells and their multiple signaling pathways by triggering calcium mobilization, activation of Rho GTPases, MAPK, and NFκB that control diverse host cells functions and behaviors, including cytoskeleton remodeling [9].…”

Section: Introductionmentioning

confidence: 99%

“…Despite the absence of an effect on adhesion, inactivation of the sprR gene leads to an increase in the invasive activity of S. proteamaculans correlated with the increase in the activity of extracellular metalloprotease serralysin, which is cytotoxic to mammalian cells. In addition, the inactivation of the sprR gene as well as inactivation of the sprI gene [6] results in a loss of the S. proteamaculans' ability to adapt to iron-limiting conditions. This can be a key factor in influencing the spread of infection in the body, because iron content in the body is limited during infections due to sequestration by host proteins such as lactoferrin, transferrin, and haemoglobin.…”

Section: Introductionmentioning

confidence: 99%

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The Role of SprIR Quorum Sensing System in the Regulation of Serratia proteamaculans 94 Invasion

et al. 2021

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The bacteria Serratia proteamaculans 94 have a LuxI/LuxR type QS system consisting of AHL synthase SprI and the regulatory receptor SprR. We have previously shown that inactivation of the AHL synthase sprI gene resulted in an increase in the invasive activity of S. proteamaculans correlated with an increased bacterial adhesion. In the present work, the effects of inactivation of the S. proteamaculans receptor SprR are studied. Our results show that inactivation of the receptor sprR gene leads to an increase in bacterial invasion without any increase in their adhesion. On the other hand, inactivation of the sprR gene increases the activity of the extracellular protease serralysin. Inactivation of the QS system does not affect the activity of the pore-forming toxin ShlA and prevents the ShlA activation under conditions of a limited concentration of iron ions typical of the human body. While the wild type strain shows increased invasion in the iron-depleted medium, deletion of its QS system leads to a decrease in host cell invasion, which is nevertheless similar to the level of the wild type S. proteamaculans grown in the iron-rich medium. Thus, inactivation of either of the two component of the S. proteamaculans LuxI/LuxR-type QS system leads to an increase in the invasive activity of these bacteria through different mechanisms and prevents invasion under the iron-limited conditions.

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Section: Introductioncontrasting

confidence: 57%

Section: Introductionsupporting

confidence: 51%

Section: The Effects Of the Receptor Sprr Gene Inactivation On The S Proteamaculans Invasive Activitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Role of SprIR Quorum Sensing System in the Regulation of Serratia proteamaculans 94 Invasion

et al. 2021

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Bacterial Outer Membrane Protein OmpX Regulates β1 Integrin and Epidermal Growth Factor Receptor (EGFR) Involved in Invasion of M-HeLa Cells by Serratia proteamaculans

Tsaplina

Bozhokina

2021

IJMS

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Opportunistic pathogen Serratia proteamaculans are able to penetrate the eukaryotic cells. The penetration rate can be regulated by bacterial surface protein OmpX. OmpX family proteins are able to bind to host cell surface to the epidermal growth factor receptor (EGFR) and the extracellular matrix protein fibronectin, whose receptors are in return the α5 β1 integrins. Here we elucidated the involvement of these host cell proteins in S. proteamaculans invasion. We have shown that, despite the absence of fibronectin contribution to S. proteamaculans invasion, β1 integrin was directly involved in invasion of M-HeLa cells. Herewith β1 integrin was not the only receptor that determines sensitivity of host cells to bacterial invasion. Signal transfer from EGFR was also involved in the penetration of these bacteria into M-HeLa cells. However, M-HeLa cells have not been characterized by large number of these receptors. It turned out that S. proteamaculans attachment to the host cell surface resulted in an increment of EGFR and β1 integrin genes expression. Such gene expression increment also caused Escherichia coli attachment, transformed with a plasmid encoding OmpX from S. proteamaculans. Thus, an OmpX binding to the host cell surface caused an increase in the EGFR and β1 integrin expression involved in S. proteamaculans invasion.

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Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA

Tsaplina

Khaitlina

Chukhontseva

et al. 2022

IJMS

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Serratia proteamaculans synthesizes the intracellular metalloprotease protealysin. This work was aimed at searching for bacterial substrates of protealysin among the proteins responsible for replication and cell division. We have shown that protealysin unlimitedly cleaves the SOS response protein RecA. Even 20% of the cleaved RecA in solution appears to be incorporated into the polymer of uncleaved monomers, preventing further polymerization and inhibiting RecA ATPase activity. Transformation of Escherichia coli with a plasmid carrying the protealysin gene reduces the bacterial UV survival up to 10 times. In addition, the protealysin substrate is the FtsZ division protein, found in both E. coli and Acholeplasma laidlawii, which is only 51% identical to E. coli FtsZ. Protealysin cleaves FtsZ at the linker between the globular filament-forming domain and the C-terminal peptide that binds proteins on the bacterial membrane. Thus, cleavage of the C-terminal segment by protealysin can lead to the disruption of FtsZ’s attachment to the membrane, and thereby inhibit bacterial division. Since the protealysin operon encodes not only the protease, but also its inhibitor, which is typical for the system of interbacterial competition, we assume that in the case of penetration of protealysin into neighboring bacteria that do not synthesize a protealysin inhibitor, cleavage of FtsZ and RecA by protealysin may give S. proteamaculans an advantage in interbacterial competition.

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Invasion of Serratia proteamaculans is regulated by the sprI gene encoding AHL synthase

Cited by 4 publications

References 27 publications

The Role of SprIR Quorum Sensing System in the Regulation of Serratia proteamaculans 94 Invasion

The Role of SprIR Quorum Sensing System in the Regulation of Serratia proteamaculans 94 Invasion

Bacterial Outer Membrane Protein OmpX Regulates β1 Integrin and Epidermal Growth Factor Receptor (EGFR) Involved in Invasion of M-HeLa Cells by Serratia proteamaculans

Protealysin Targets the Bacterial Housekeeping Proteins FtsZ and RecA

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